Please use this identifier to cite or link to this item:
標題: 犬精漿基質金屬蛋白酵素2及9之分析
Detection of Matrix Metalloproteinase (MMP)-2 and MMP-9 in Canine Seminal Plasma
作者: 范巾賢
Saengsoi, Wipawee
關鍵字: Canine;犬;Matrix metalloproteinase;Seminal plasma;Sperm quality;基質金屬蛋白酵素;精漿;精蟲品質
出版社: 獸醫學系暨研究所
引用: REFERENCES Asadpour R, Alavi-Shoushtari SM, Rezaii SA, Ansari MH. SDS-polyacrylamide gel electrophoresis of buffalo bulls seminal plasma proteins and their relation with semen freezability. Anim Reprod Sci 102: 308-13, 2007. Astedt B, Bladh B, Holmberg L, Liedholm P. Purification of plasminogen activator(s) from human seminal plasma. Experientia 32: 148-9, 1976. Aziz N, Said T, Paasch U, Agarwal A. The relationship between human sperm apoptosis, morphology and the sperm deformity index. Hum Reprod 22: 1413-1419, 2007. Bartholome EJ, Van Aelst I, Koyen E, Kiss R, Willems F, Goldman M, Opdenakker G. Human monocyte-derived dendritic cells produce bioactive gelatinase B: inhibition by IFN-beta. J Interferon Cytokine Res 21: 495-501, 2001. Baumgart E, Lenk SV, Loening SA, Jung K. Quantitative differences in matrix metalloproteinase (MMP)-2, but not in MMP-9, tissue inhibitor of metalloproteinase (TIMP)-1 or TIMP-2, in seminal plasma of normozoospermic and azoospermic patients. Hum Reprod 17: 2919-23, 2002. Bergers G, Brekken R, McMahon G, Vu TH, Itoh T, Tamaki K, Tanzawa K, Thorpe P, Itohara S, Werb Z, Hanahan D. Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol 2: 737-44, 2000. Birkedal-Hansen H, Taylor RE. Detergent-activation of latent collagenase and resolution of its component molecules. Biochem Biophys Res Commun 107: 1173-8, 1982. Bode W. Structural basis of matrix metalloproteinase function. Biochem Soc Symp : 1-14, 2003. Bonde JP, Ernst E, Jensen TK, Hjollund NH, Kolstad H, Henriksen TB, Scheike T, Giwercman A, Olsen J, Skakkebaek NE. Relation between semen quality and fertility: a population-based study of 430 first-pregnancy planners. Lancet 352: 1172-7, 1998. Brandon CI, Heusner GL, Caudle AB, Fayrer-Hosken RA. Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility. Theriogenology 52: 863-73, 1999. Brooks DE. Androgen-regulated epididymal secretory proteins associated with post-testicular sperm development. Ann N Y Acad Sci 513: 179-94, 1987. Brown PD, Bloxidge RE, Anderson E, Howell A. Expression of activated gelatinase in human invasive breast carcinoma. Clin Exp Metastasis 11: 183-9, 1993. Brown PD, Levy AT, Margulies IM, Liotta LA, Stetler-Stevenson WG. Independent expression and cellular processing of Mr 72,000 type IV collagenase and interstitial collagenase in human tumorigenic cell lines. Cancer Res 50: 6184-91, 1990. Buchman-Shaked O, Kraiem Z, Gonen Y, Goldman S. Presence of matrix metalloproteinases and tissue inhibitor of matrix metalloproteinase in human sperm. J Androl 23: 702-8, 2002. Calvete J, Raida M, Gentzel M, Urbanke C, Sanz L, Topfer E. Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1. FEBS Lett. 407: 201-206, 1997. Cataldo DD, Tournoy KG, Vermaelen K, Munaut C, Foidart JM, Louis R, Noel A, Pauwels RA. Matrix metalloproteinase-9 deficiency impairs cellular infiltration and bronchial hyperresponsiveness during allergen-induced airway inflammation. Am J Pathol 161: 491-8, 2002. Chambers AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst 89: 1260-70, 1997. Cho A, Reidy MA. Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury. Circ Res 91: 845-51, 2002. Cross NL. Multiple effects of seminal plasma on the acrosome reaction of human sperm. Mol Reprod Dev 35: 316-323, 1993. de Souza FF, Barreto CS, Lopes MD. Characteristics of seminal plasma proteins and their correlation with canine semen analysis. Theriogenology 68: 100-6, 2007. Delella FK, Justulin LA, Jr., Felisbino SL. Tissue inhibitor of metalloproteinase-2 (TIMP-2) location in the ventral, lateral, dorsal and anterior lobes of rat prostate by immunohistochemistry. Cell Biol Int 31: 229-34, 2007. Ducharme A, Frantz S, Aikawa M, Rabkin E, Lindsey M, Rohde LE, Schoen FJ, Kelly RA, Werb Z, Libby P, Lee RT. Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction. J Clin Invest 106: 55-62, 2000. Edwards JJ, Tollaksen SL, Anderson NG. Proteins of human semen. I. Two-dimensional mapping of human seminal fluid. Clin Chem 27: 1335-40, 1981. Engsig MT, Chen QJ, Vu TH, Pedersen AC, Therkidsen B, Lund LR, Henriksen K, Lenhard T, Foged NT, Werb Z, Delaisse JM. Matrix metalloproteinase 9 and vascular endothelial growth factor are essential for osteoclast recruitment into developing long bones. J Cell Biol 151: 879-89, 2000. Erickson-Lawrence M, Zabludoff SD, Wright WW. Cyclic protein-2, a secretory product of rat Sertoli cells, is the proenzyme form of cathepsin L. Mol Endocrinol 5: 1789-98, 1991. Fowlkes JL, Winkler MK. Exploring the interface between metallo-proteinase activity and growth factor and cytokine bioavailability. Cytokine Growth Factor Rev 13: 277-87, 2002. Franken DR, Bastiaan HS, Kidson A, Wranz P, Habenicht UF. Zona pellucida mediated acrosome reaction and sperm morphology. Andrologia 29: 311-7, 1997. Freshman JL. Semen collection and evaluation. Clin Tech Small Anim Pract 17: 104-7, 2002. Galis ZS, Johnson C, Godin D, Magid R, Shipley JM, Senior RM, Ivan E. Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling. Circ Res 91: 852-9, 2002. Garg P, Vijay-Kumar M, Wang L, Gewirtz AT, Merlin D, Sitaraman SV. Matrix metalloproteinase-9-mediated tissue injury overrides the protective effect of matrix metalloproteinase-2 during colitis. Am J Physiol Gastrointest Liver Physiol 296: 175-84, 2009. Ghaddar G, Ruchon AF, Carpentier M, Marcinkiewicz M, Seidah NG, Crine P, Desgroseillers L, Boileau G. Molecular cloning and biochemical characterization of a new mouse testis soluble-zinc-metallopeptidase of the neprilysin family. Biochem J 347: 419-29, 2000. Gunalp S, Onculoglu C, Gurgan T, Kruger TF, Lombard CJ. A study of semen parameters with emphasis on sperm morphology in a fertile population: an attempt to develop clinical thresholds. Hum Reprod 16: 110-114, 2001. Gunnarsson M, Lecander I, Abrahamsson PA. Factors of the plasminogen activator system in human testis, as demonstrated by in-situ hybridization and immunohistochemistry. Mol Hum Reprod 5: 934-40, 1999. Hassan MI, Kumar V, Kashav T, Alam N, Singh TP, Yadav S. Proteomic approach for purification of seminal plasma proteins involved in tumor proliferation. J Sep Sci 30: 1979-88, 2007. Heissig B, Hattori K, Dias S, Friedrich M, Ferris B, Hackett NR, Crystal RG, Besmer P, Lyden D, Moore MA, Werb Z, Rafii S. Recruitment of stem and progenitor cells from the bone marrow niche requires MMP-9 mediated release of kit-ligand. Cell 109: 625-37, 2002. Henalut, M.A, Killian, GJ, Kavanaaugh, JF, Gril, LC. Effect of accessory sex gland fluid from bulls of different fertilities on the ability of caudu epididymal sperm to penetrate zona-free ovine oocytes. Biol Reprod 52: 390-397, 1995. Heymans S, Luttun A, Nuyens D, Theilmeier G, Creemers E, Moons L, Dyspersin GD, Cleutjens JP, Shipley M, Angellilo A, Levi M, Nube O, Baker A, Keshet E, Lupu F, Herbert JM, Smits JF, Shapiro SD, Baes M, Borgers M, Collen D, Daemen MJ, Carmeliet P. Inhibition of plasminogen activators or matrix metalloproteinases prevents cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure. Nat Med 5: 1135-42, 1999. Hinton BT, Palladino MA, Rudolph D, Labus JC. The epididymis as protector of maturing spermatozoa. Reprod Fertil Dev 7: 731-45, 1995. Hoeben E, Van Aelst I, Swinnen JV, Opdenakker G, Verhoeven G. Gelatinase A secretion and its control in peritubular and Sertoli cell cultures: effects of hormones, second messengers and inducers of cytokine production. Mol Cell Endocrinol 118: 37-46, 1996. Hulboy DL, Rudolph LA, Matrisian LM. Matrix metalloproteinases as mediators of reproductive function. Mol Hum Reprod 3: 27-45, 1997. Itoh T, Tanioka M, Matsuda H, Nishimoto H, Yoshioka T, Suzuki R, Uehira M. Experimental metastasis is suppressed in MMP-9-deficient mice. Clin Exp Metastasis 17: 177-81, 1999. Jobim MIM, Oberst ER, Salbego CG, Wald VB, Horn AP, Mattos RC. BSP A1/A2 like proteins in ram seminal plasma. Theriogenology 63: 2053-2062, 2005. Jonakova V, Manaskova P, Ticha M. Separation, characterization and identification of boar seminal plasma proteins. J Chromatogr B Analyt Technol Biomed Life Sci 849: 307-14, 2007. Kawai K, Uetsuka K, Doi K, Nakayama H. The activity of matrix metalloproteinases (MMPS) and tissue inhibitors of metalloproteinases (TIMPs) in mammary tumors of dogs and rats. J Vet Med Sci 68: 105-11, 2006. Killian GJ, Chapman DA, Rogowski LA. Fertility-associated proteins in Holstein bull seminal plasma. Biol Reprod 49: 1202-7, 1993. Kirchhoff C. Molecular characterization of epididymal proteins. Rev Reprod 3: 86-95, 1998. Kleiner DE, Stetler-Stevenson WG. Quantitative zymography: detection of picogram quantities of gelatinases. Anal Biochem 218: 325-9, 1994. Kohno N, Yamagata K, Yamada S, Kashiwabara S, Sakai Y, Baba T. Two novel testicular serine proteases, TESP1 and TESP2, are present in the mouse sperm acrosome. Biochem Biophys Res Commun 245: 658-65, 1998. Konttinen YT, Ceponis A, Takagi M, Ainola M, Sorsa T, Sutinen M, Salo T, Ma J, Santavirta S, Seiki M. New collagenolytic enzymes/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: destruction from above. Matrix Biol 17: 585-601, 1998. Kruger TF, Acosta AA, Simmons KF, Swanson RJ, Matta JF, Oehninger S. Predictive value of abnormal sperm morphology in in vitro fertilization. Fertil Steril 49: 112-7, 1988. Kubo M, Matsumiya K, Iwamoto T, Kaneko S, Ishijima S. Morphological abnormalities in the spermatozoa of fertile and infertile men. Mol Reprod Dev 70: 70-81, 2005. Lazure C, Leduc R, Seidah NG, Chretien M, Dube JY, Chapdelaine P, Frenette G, Paquin R, Tremblay RR. The major androgen-dependent protease in dog prostate belongs to the kallikrein family: confirmation by partial amino acid sequencing. FEBS Lett 175: 1-7, 1984. Lelongt B, Bengatta S, Delauche M, Lund LR, Werb Z, Ronco PM. Matrix metalloproteinase 9 protects mice from anti-glomerular basement membrane nephritis through its fibrinolytic activity. J Exp Med 193: 793-802, 2001. Lessley BA, Garner DL. Identification and distribution of Pz-peptidases A and B in human semen. J Androl 6: 372-8, 1985. Liu Z, Shapiro SD, Zhou X, Twining SS, Senior RM, Giudice GJ, Fairley JA, Diaz LA. A critical role for neutrophil elastase in experimental bullous pemphigoid. J Clin Invest 105: 113-23, 2000. Liu Z, Zhou X, Shapiro SD, Shipley JM, Twining SS, Diaz LA, Senior RM, Werb Z. The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell 102:647-55, 2000. Lokeshwar BL, Selzer MG, Block NL, Gunja-Smith Z. Secretion of matrix metalloproteinases and their inhibitors (tissue inhibitor of metalloproteinases) by human prostate in explant cultures: reduced tissue inhibitor of metalloproteinase secretion by malignant tissues. Cancer Res 53: 4493-8, 1993. Longin J, Guillaumot P, Chauvin MA, Morera AM, Le Magueresse-Battistoni B. MT1-MMP in rat testicular development and the control of Sertoli cell proMMP-2 activation. J Cell Sci 114: 2125-34, 2001. Lukac J, Koren E. Mechanism of liquefaction of the human ejaculate. II. Role of collagenase-like peptidase and seminal proteinase. J Reprod Fertil 56: 501-6, 1979. Malm J, Hellman J, Magnusson H, Laurell CB, Lilja H. Isolation and characterization of the major gel proteins in human semen, semenogelin I and semenogelin II. Eur J Biochem 238: 48-53, 1996. Mann T. Experimental approach to the study of semen and male reproductive function. Int J Fertil 23: 133-7, 1978. Mannello F, Gazzanelli G. Tissue inhibitors of metalloproteinases and programmed cell death: conundrums, controversies and potential implications. Apoptosis 6: 479-82, 2001. Mannello F, Luchetti F, Falcieri E, Papa S. Multiple roles of matrix metalloproteinases during apoptosis. Apoptosis 10: 19-24, 2005. Mannello F, Tonti G, Papa S. Matrix metalloproteinase inhibitors as anticancer therapeutics. Curr Cancer Drug Targets 5: 285-98, 2005. Mannello F, Tonti G, Bagnara GP, Papa S. Role and function of matrix metalloproteinases in the differentiation and biological characterization of mesenchymal stem cells. Stem Cells 24: 475-81, 2006. Matsumoto K, Yamauchi N, Watanabe R, Oozono S, Kubota K, Nishimura K, Wood C, Soh T, Kizaki K, Hattori MA. In vitro decidualization of rat endometrial stromal cells. Cell Tissue Res 335: 575-83, 2009. Mbikay M, Tadros H, Ishida N, Lerner CP, De Lamirande E, Chen A, El-Alfy M, Clermont Y, Seidah NG, Chretien M, Gagnon C, Simpson EM. Impaired fertility in mice deficient for the testicular germ-cell protease PC4. Proc Natl Acad Sci U S A 94: 6842-6, 1997. McCauley TC, Zhang HM, Bellin ME, Ax RL. Identification of a heparin-binding protein in bovine seminal fluid as tissue inhibitor of metalloproteinases-2. Mol Reprod Dev 58: 336-41, 2001. McGee RS, Herr JC. Human seminal vesicle-specific antigen is a substrate for prostate-specific antigen (or P-30). Biol Reprod 39: 499-510, 1988. McLean GW, Carragher NO, Avizienyte E, Evans J, Brunton VG, Frame MC. The role of focal-adhesion kinase in cancer - a new therapeutic opportunity. Nat Rev Cancer 5: 505-15, 2005. Menkveld R, Wong WY, Lombard CJ, Wetzels AM, Thomas CM, Merkus HM, Steegers-Theunissen RP. Semen parameters, including WHO and strict criteria morphology, in a fertile and subfertile population: an effort towards standardization of in-vivo thresholds. Hum Reprod 16: 1165-71, 2001. Menon B, Singh M, Ross RS, Johnson JN, Singh K. beta-Adrenergic receptor-stimulated apoptosis in adult cardiac myocytes involves MMP-2-mediated disruption of beta1 integrin signaling and mitochondrial pathway. Am J Physiol Cell Physiol 290: 254-61, 2006. Metayer S, Dacheux F, Dacheux JL, Gatti JL. Comparison, characterization, and identification of proteases and protease inhibitors in epididymal fluids of domestic mammals. Matrix metalloproteinases are major fluid gelatinases. Biol Reprod 66: 1219-1229, 2002. Miller DJ, Winer MA, Ax RL. Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin. Biol Reprod 42: 899-915, 1990. Morley ME, Riches K, Peers C, Porter KE. Hypoxic inhibition of human cardiac fibroblast invasion and MMP-2 activation may impair adaptive myocardial remodelling. Biochem Soc Trans 35: 905-7, 2007. Mott JD, Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 16: 558-64, 2004. Nagase H, Woessner JF, Jr. Matrix metalloproteinases. J Biol Chem 274: 21491-4, 1999. Nauk V, Manjunath P. Radioimmunoassays for bull seminal plasma proteins (BSP A1/A2, BSP-A3, and BSP-30 kDa), and their quantification in seminal plasma & sperm. Biol Reprod 63: 1058-1066, 2000. Newby AC. Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture. Physiol Rev 85: 1-31, 2005. Oettle EE. Sperm morphology and fertility in the dog. J Reprod Fertil Suppl 47: 257-60, 1993. Ogier C, Bernard A, Chollet AM, Le Diguardher T, Hanessian S, Charton G, Khrestchatisky M, Rivera S. Matrix metalloproteinase-2 (MMP-2) regulates astrocyte motility in connection with the actin cytoskeleton and integrins. Glia 54: 272-284, 2006. Okada Y, Gonoji Y, Naka K, Tomita K, Nakanishi I, Iwata K, Yamashita K, Hayakawa T. Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties. J Biol Chem 267: 21712-9, 1992. Olar TT, Amann RP, Pickett BW. Relationships among testicular size, daily production and output of spermatozoa, and extragonadal spermatozoal reserves of the dog. Biol Reprod 29: 1114-20, 1983. Ombelet W, Bosmans E, Janssen M, Cox A, Vlasselaer J, Gyselaers W, Vandeput H, Gielen J, Pollet H, Maes M, Steeno O, Kruger T. Semen parameters in a fertile versus subfertile population: a need for change in the interpretation of semen testing. Hum Reprod 12: 987-93, 1997. Parsons SL, Watson SA, Brown PD, Collins HM, Steele RJ. Matrix metalloproteinases. Br J Surg 84: 160-6, 1997. Perez SE, Cano DA, Dao-Pick T, Rougier JP, Werb Z, Hebrok M. Matrix metalloproteinases 2 and 9 are dispensable for pancreatic islet formation and function in vivo. Diabetes 54: 694-701, 2005. Pyo R, Lee JK, Shipley JM, Curci JA, Mao D, Ziporin SJ, Ennis TL, Shapiro SD, Senior RM, Thompson RW. Targeted gene disruption of matrix metalloproteinase-9 (gelatinase B) suppresses development of experimental abdominal aortic aneurysms. J Clin Invest 105: 1641-9, 2000. Reese JH, McNeal JE, Redwine EA, Samloff IM, Stamey TA. Differential distribution of pepsinogen II between the zones of the human prostate and the seminal vesicle. J Urol 136: 1148-52, 1986. Remondino A, Kwon SH, Communal C, Pimentel DR, Sawyer DB, Singh K, Colucci WS. Beta-adrenergic receptor-stimulated apoptosis in cardiac myocytes is mediated by reactive oxygen species/c-Jun NH2-terminal kinase-dependent activation of the mitochondrial pathway. Circ Res 92: 136-8, 2003. Ricci G, Perticarari S, Fragonas E, Giolo E, Canova S, Pozzobon C, Guaschino S, Presani G. Apoptosis in human sperm: its correlation with semen quality and the presence of leukocytes. Hum Reprod 17: 2665-2672, 2002. Robinson LL, Sznajder NA, Riley SC, Anderson RA. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human fetal testis and ovary. Mol Hum Reprod 7: 641-8, 2001. Romanic AM, Harrison SM, Bao W, Burns-Kurtis CL, Pickering S, Gu J, Grau E, Mao J, Sathe GM, Ohlstein EH, Yue TL. Myocardial protection from ischemia/reperfusion injury by targeted deletion of matrix metalloproteinase-9. Cardiovasc Res 54: 549-58, 2002. Root Kustritz MV. The value of canine semen evaluation for practitioners. Theriogenology 68: 329-37, 2007. Rudolph-Owen LA, Cannon P, Matrisian LM. Overexpression of the matrix metalloproteinase matrilysin results in premature mammary gland differentiation and male infertility. Mol Biol Cell 9: 421-35, 1998. Russell DL, Salamonsen LA, Findlay JK. Immunization against the N-terminal peptide of the inhibin alpha 43-subunit (alpha N) disrupts tissue remodeling and the increase in matrix metalloproteinase-2 during ovulation. Endocrinology 136: 3657-64, 1995. Salamonsen LA, Woolley DE. Matrix metalloproteinases in normal menstruation. Hum Reprod 11 Suppl 2: 124-33, 1996. Sang QX, Dym M, Byers SW. Secreted metalloproteinases in testicular cell culture. Biol Reprod 43: 946-55, 1990. Sheu BC, Hsu SM, Ho HN, Lien HC, Huang SC, Lin RH. A novel role of metalloproteinase in cancer-mediated immunosuppression. Cancer Res 61: 237-42, 2001. Shimokawa Ki K, Katayama M, Matsuda Y, Takahashi H, Hara I, Sato H, Kaneko S. Matrix metalloproteinase (MMP)-2 and MMP-9 activities in human seminal plasma. Mol Hum Reprod 8: 32-6, 2002. Somerville RP, Oblander SA, Apte SS. Matrix metalloproteinases: old dogs with new tricks. Genome Biol 4: 216, 2003. Stamenkovic I. Extracellular matrix remodelling: the role of matrix metalloproteinases. J Pathol 200: 448-64, 2003. Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 17: 463-516, 2001. Tentes I, Asimakopoulos B, Mourvati E, Diedrich K, Al-Hasani S, Nikolettos N. Matrix metalloproteinase (MMP)-2 and MMP-9 in seminal plasma. J Assist Reprod Genet 24: 278-81, 2007. Tulsiani DR, Abou-Haila A, Loeser CR, Pereira BM. The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp Cell Res 240: 151-64, 1998. Uhrin P, Dewerchin M, Hilpert M, Chrenek P, Schofer C, Zechmeister-Machhart M, Kronke G, Vales A, Carmeliet P, Binder BR, Geiger M. Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility. J Clin Invest 106: 1531-9, 2000. Ulisse S, Farina AR, Piersanti D, Tiberio A, Cappabianca L, D''Orazi G, Jannini EA, Malykh O, Stetler-Stevenson WG, D''Armiento M. Follicle-stimulating hormone increases the expression of tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 and induces TIMP-1 AP-1 site binding complex(es) in prepubertal rat Sertoli cells. Endocrinology 135: 2479-87, 1994. Villemure M, Lazure C, Manjunath P. Isolation and characterization of gelatin-binding proteins from goat seminal plasma. Reprod Biol Endocrinol 1: 39-50, 2003. Vu TH, Shipley JM, Bergers G, Berger JE, Helms JA, Hanahan D, Shapiro SD, Senior RM, Werb Z. MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell 93: 411-22, 1998. Vu TH, Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 14: 2123-33, 2000. Wang M, Qin X, Mudgett JS, Ferguson TA, Senior RM, Welgus HG. Matrix metalloproteinase deficiencies affect contact hypersensitivity: stromelysin-1 deficiency prevents the response and gelatinase B deficiency prolongs the response. Proc Natl Acad Sci USA 96: 6885-9, 1999. Werb Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91: 439-42, 1997. Wilson MJ, Garcia B, Woodson M, Sinha AA. Metalloproteinase activities expressed during development and maturation of the rat prostatic complex and seminal vesicles. Biol Reprod 47: 683-91, 1992. Wilson MJ, Norris H, Kapoor D, Woodson M, Limas C, Sinha AA. Gelatinolytic and caseinolytic proteinase activities in human prostatic secretions. J Urol 149: 653-8, 1993. Wilson MJ, Strasser M, Vogel MM, Sinha AA. Calcium-dependent and calcium-independent gelatinolytic proteinase activities of the rat ventral prostate and its secretion: characterization and effect of castration and testosterone treatment. Biol Reprod 44: 776-85, 1991. Woessner JFJ. The family of matrix metalloproteinases. Ann N Y Acad Sci 732: 11-21, 1994. Wohlschlaeger J, Stubbe HD, Schmitz KJ, Kawaguchi N, Takeda A, Takeda N, Hinder F, Baba HA. Roles of MMP-2/-9 in cardiac dysfunction during early multiple organ failure in an ovine animal model. Pathol Res Pract 201: 809-17, 2005. Xu P, Wang YL, Zhu SJ, Luo SY, Piao YS, Zhuang LZ. Expression of matrix metalloproteinase-2, -9, and -14, tissue inhibitors of metalloproteinase-1, and matrix proteins in human placenta during the first trimester. Biol Reprod 62: 988-94, 2000. Yamagata K, Murayama K, Okabe M, Toshimori K, Nakanishi T, Kashiwabara S, Baba T. Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction. J Biol Chem 273: 10470-4, 1998. Yin HZ, Vogel MM, Schneider M, Ercole C, Zhang G, Sinha AA, Wilson MJ. Gelatinolytic proteinase activities in human seminal plasma. J Reprod Fertil 88: 491-501, 1990. Zhang K, McQuibban GA, Silva C, Butler GS, Johnston JB, Holden J, Clark-Lewis I, Overall CM, Power C. HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration. Nat Neurosci 6:1064-71, 2003. Zheng X, Geiger M, Ecke S, Bielek E, Donner P, Eberspacher U, Schleuning WD, Binder BR. Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa. Am J Physiol 267: 466-72, 1994.
精漿包含許多由睪丸、前列腺、及其他附屬性腺細胞來源的蛋白酶,如膠原蛋白酶樣胜肽酶(collagenase-like peptidase)、明膠分解蛋白酶(gelatinolytic proteinases)、胞漿素原活化劑(plasminogen activator)、第二型胃蛋白酶原(pepsinogen II)、Pz-胜肽酶(Pz-peptidase)及前列腺特殊抗原。基質金屬蛋白酵素(matrix metalloproteinases, MMPs)是屬於蛋白溶解酵素家族之一,並且包含了膠原蛋白酶樣胜肽酶及明膠分解蛋白酶。MMPs可分解細胞外基質及基底膜上的蛋白質;此特性可能與細胞增生、移形、分化、血管新生、凋亡及宿主防禦相關的細胞活動有關。先前文獻已證實,在人的精漿中有MMP-2(72 kDa)及MMP-9(92 kDa)兩種MMPs,並且亦少述探討各種MMPs存在於犬隻精漿的文獻。然而,此類MMP濃度與精液品質之間的關係仍為目前未釐清的課題。本研究目的在評估犬精液樣本中,非活化態(latent)與活化態(active)MMP-2及MMP-9活性和影響精液品質的相關因子之間是否具有相關性。本研究結果發現非活化態與活化態MMP-2及MMP-9皆存在於犬精液樣本(=49)中,並且以非活化態的形式存在為主;而在與精液品質的關係上,具有低精子濃度、低總精子數、低正常形態精子數、低正常形態活精子數的樣本中,非活化態與活化態的MMP-9的活性皆較高。此外,非活化態MMP-9活性和總精液量、精子總存活數、正常形態的活精子百分比數值間呈現負相關。非活化態MMP-2和總精液量、精子存活百分比與正常形態精子數間同樣呈現負相關;活化態MMP-2則和具有活動力精子數與具有活動力且具有正常型態的精子數呈現負相關。本實驗指出proMMP-9和MMP-9的活性可能是精液品質低下繁殖力之原因或造成之結果。由於MMP-2活性和精子的高運動性有緊密關係,因此進一步研究有待證實MMP-2的活性是否可用來評估精子功能或當成雄性繁殖能力之有效指標。

Seminal plasma contains many proteinases originating from testicular cells, prostate and other accessory sex glands, such as collagenase-like peptidase, gelatinolytic proteinases, plasminogen activator, pepsinogen II, Pz-peptidase and prostatic specific antigen. The matrix metalloproteinases (MMPs), which contain collagenase-like peptidase and gelatinolytic proteinase activities, are a family of proteolytic enzymes that degrade protein components of the extracellular matrix and basement membrane. Therefore, they might be involved in cell behaviors such as cell proliferation, migration, differentiation, angiogenesis, apoptosis and host defense. Previous studies have shown that MMP-2 and MMP-9, known as 72 kDa and 92 kDa gelatinase or type Ⅳ collagenase respectively, were presented in human seminal plasma. One of the main questions is whether the levels of MMPs are associated with semen traits. Following the line of research, only few studies have been focused on the presence of MMPs in canine seminal plasma. Aims of this study were to evaluate the latent and active forms of MMP-2 and MMP-9 in this species and to investigate their association with semen parameters. The results (n=49) have shown that both latent and active forms of MMP-2 and MMP-9 were present in canine seminal plasma, and latent forms were the predominant proteins. Interestingly, the high latent and active forms of MMP-9 activity were elevated in semen with low sperm count of concentration, normal morphology, and normal live sperm. Furthermore, there were inverse correlation between the levels of proMMP-9 with semen volume, total count of vital sperm, and % normal live sperm; proMMP-2 with semen volume, % vital sperm, and normal sperm whereas MMP-2 was positively correlated with total count of motile sperm, and normal motile sperm. These findings infer that the role of proMMP-9 and MMP-9 activation may contribute to, at least in part, the cause of poor semen quality. For the reason that MMP-2 activity is intimately associated with high sperm motility, the activation of MMP-2 might improve or be indicators of sperm functionality.
其他識別: U0005-0707200915351500
Appears in Collections:獸醫學系所

Show full item record

Google ScholarTM


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.