Hostname: page-component-8448b6f56d-cfpbc Total loading time: 0 Render date: 2024-04-20T02:35:24.664Z Has data issue: false hasContentIssue false
  • English
  • Français

Regional accretion of gelatinase B in mammary gland during gradual and acute involution of dairy animals

Published online by Cambridge University Press:  12 May 2008

Ming H Weng ,
Ting C Yu ,
Shuen E Chen ,
Ho C Peh ,
Wen B Liu ,
Ming T Chen ,
Hajemi Nagahata  and
Chai J Chang
Ming H Weng
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung402, TaiwanROC
Ting C Yu
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung402, TaiwanROC
Shuen E Chen
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung402, TaiwanROC
Ho C Peh
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung402, TaiwanROC
Wen B Liu
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung402, TaiwanROC
Ming T Chen
Affiliation:
Department of Bioindustry Technology, Da Yeh University, Chung Hwa515, TaiwanROC
Hajemi Nagahata
Affiliation:
Department of Animal Health, School of Veterinary Medicine, Rakuno Gakuen University, Ebetsu, Hokkaido069-8501, Japan
Chai J Chang*
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung402, TaiwanROC
*
†For correspondence; e-mail: crchang@mail.nchu.edu.tw
Get access Rights & Permissions [Opens in a new window]

Abstract

The level of gelatinases in surrounding body fluids of actively remodelling tissue is indicative of basement membrane and extracellular matrix degradation under various physiological and pathological circumstances. To elucidate the association of gelatinase with mammary tissue remodelling during gradual or acute involution, in the first trial, goats milked twice daily (lactation) and goats receiving decreased milking frequency (involution) served to provide a total of 12 milk samples and 11 mammary secretion samples, respectively. In the second trial, 6 cows served to provide samples of dry secretion in 3 consecutive weeks immediately following milk stasis. Gelatin zymography was applied for gelatinase phenotyping and quantification on milk, plasma and the degranulation medium/lysate of milk somatic cells. Results indicated that the most prevalent gelatinase subtype switched from gelatinase A in milk to gelatinase B in involution secretion. Mammary secretion of goats during involution contained marginally higher protein level, significantly lower casein ratio and greater specific capacity of gelatinase B compared with those of milk during lactation. Specific capacities of gelatinases A and B in plasma of goats were similar during lactation and involution, while gelatinase B capacity in degranulation medium/lysates based on unit number of goat somatic cell was significantly higher during involution than during lactation. Milk stasis of cows induced a significant increase in specific capacity of gelatinase B, but not gelatinase A, of dry secretion up to the third week. Results of both trials agree that regional selective accretion of gelatinase B in milk might have played a role in mammary tissue remodelling during involution induced by either decreasing milking frequency or milk stasis. It is suggested that infiltrated polymorphonuclear neutrophils are one of the potential contributors responsible for the accumulation of gelatinase B during involution.

Keywords

Gelatinase specific capacitymammary gland involutionsomatic cellsgoatscows
Type
Research Article
Information
Journal of Dairy Research , Volume 75 , Issue 2 , May 2008 , pp. 202 - 210
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Akers, RM 2002 Overview of mammary development. In: Lactation and the Mammary Gland (Ed. Akers, RM) pp. 38–44. Ames IO, USA: Iowa State PressGoogle Scholar
Annabi, B, Currie, JC, Moghrabi, A & Beliveau, R 2007 Inhibition of HuR and MMP-9 expression in macrophage-differentiated HL-60 myeloid leukemia cells by green tea polyphenol EGCg. Leukemia Research 31 1277–1284CrossRefGoogle ScholarPubMed
Annen, EL, Collier, RJ, McGuire, MA & Vicini, JL 2004 Effects of dry period length on milk yield and mammary epithelial cells. Journal of Dairy Science 87 E66–E76CrossRefGoogle Scholar
Annen, EL, Fitzgerald, AC, Gentry, PC, McGuire, MA, Capuco, AV, Baumgard, LH & Collier, RJ 2007 Effect of continuous milking and bovine somatotropin supplementation on mammary epithelial cell turnover. Journal of Dairy Science 90 165–183CrossRefGoogle ScholarPubMed
Atkinson, JJ & Senior, RM 2003 Matrix metalloproteinase in lung remodeling. American Journal of Respiratory and Cell Molecular Biology 28 12–24CrossRefGoogle ScholarPubMed
Bradford, MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 248–254CrossRefGoogle ScholarPubMed
Capuco, AV & Akers, RM 1999 Mammary involution in dairy animals. Journal of Mammary Gland Biology and Neoplasia 4 137–144CrossRefGoogle ScholarPubMed
Capuco, AV, Wood, DL, Baldwin, R, McLeod, K & Paape, MJ 2001 Mammary cell mumber, proliferation, and apoptosis during a bovine lactation:Relation to milk production and effect of bST. Journal of Dairy Science 84 2177–2187CrossRefGoogle Scholar
Chen, WY, Weng, MH, Chen, SE, Peh, HC, Liu, WB, Yu, TC, Huang, MC, Chen, MT, Nagahata, H & Chang, CJ 2007 Profile of gelatinolytic capacity in raw goat milk and the implication for milk quality. Journal of Dairy Science 90 4954–4965CrossRefGoogle ScholarPubMed
Cuzner, ML & Opdenakker, G 1999 Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system. Journal of Neuroimmunology 94 1–14CrossRefGoogle ScholarPubMed
Donadio, AC, Durand, S, Remedi, MM, Frede, S, Ceschin, DG, Genti-Raimondi, S & Chiabrando, GA 2005 Evaluation of stromal metalloproteinases and vascular endothelial growth factors in a spontaneous metastasis model. Experimental and Molecular Pathology 79 259–264CrossRefGoogle Scholar
Faurschou, M & Borregaard, N 2003 Neutrophil granules and secretory vesicles in inflammation. Microbes Infection 14 1317–1327CrossRefGoogle Scholar
Grummer, RR & Rastani, RR 2004 Why re-evaluate dry period length? Journal of Dairy Scienc 87 E77–E85CrossRefGoogle Scholar
Holst, BD, Hurley, WL & Nelson, DR 1987 Involution of the bovine mammary gland: histological and ultrastructural changes. Journal of Dairy Science 70 935–944CrossRefGoogle ScholarPubMed
Jeong, MA, Lee, KW, Yoon, DY & Lee, HJ 2007 Jaceosidin, a pharmacologically active flavone derived from Artemisia argyi, inhibits phorbol-ester-induced upregulation of COX-2 and MMP-9 by blocking phosphorylation of ERK-1 and -2 in cultured human mammary epithelial cells. Annals of the New York Academy of Sciences 1095 458–466CrossRefGoogle ScholarPubMed
Jouglin, M, Robert, C, Valette, J, Gavard, F, Quintin-Colonna, F & Denoix, J 2000 Metalloproteinases and tumor necrosis factor-alpha activities in synovial fluids of horses: correlation with articular cartilage alterations. Veterinary Research 31 507–515CrossRefGoogle ScholarPubMed
Laemmli, UK 1970 Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature 227 680–685CrossRefGoogle ScholarPubMed
Makowski, GS & Ramsby, ML 1996 Calibrating gelatin zymograms with human gelatinase standards. Analytical Biochemistry 236 353–356CrossRefGoogle ScholarPubMed
Makowski, GS & Ramsby, ML 2003 Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: correlation to polymorphonuclear leukocyte infiltration and in response to infection. Clinica Chimica Acta 329 77–81CrossRefGoogle ScholarPubMed
Owen, CA & Campbell, EJ 1999 The cell biology of leukocyte-mediated proteolysis. Journal of Leukocyte Biology 65 137–150CrossRefGoogle ScholarPubMed
Page-McCaw, A, Ewald, AJ & Werb, Z 2007 Matrix metalloproteinases and the regulation of tissue remodeling. Nature Reviews Molecular Cell Biology 8 221–233CrossRefGoogle Scholar
Raulo, SM, Sorsa, T, Tervahartiala, T, Latvanen, T, Pirila, E, Hirvonen, J & Maisi, P 2002 Increase in milk metalloproteinase activity and vascular permeability in bovine endotoxin-induced and naturally occurring Escherichia coli mastitis. Veterinary Immunology and Immunopathology 85 137–145CrossRefGoogle ScholarPubMed
Renner, M 1982 In: Milk and Milk Products in Human Nutrition. Munich, Germany: Vdkswirtsch, Verlag GmbH PublisherGoogle Scholar
Salama, AAK, Caja, G, Such, X, Casals, R & Albanell, E 2005 Effect of pregnancy and extended lactation on milk production in dairy goats milked once daily. Journal of Dairy Science 88 3894–3904CrossRefGoogle ScholarPubMed
Sanchez, A, Sierra, D, Luengo, C, Corrales, JC, Morales, CT, Contreras, A & Gonzalo, C 2006 Influence of storage and preservation on fossomatic cell count and composition of goat milk. Journal of Dairy Science 88 3095–3100CrossRefGoogle Scholar
Sordillo, LM & Nickerson, SC 1988 Morphologic changes in the bovine mammary gland during involution and lactogenesis. American Journal of Veterinary Research 49 1112–1120Google ScholarPubMed
Shuster, DE, Lee, EK & Kehrli, ME 1996 Bacterial growth, inflammatory cytokine production and neutrophil recruitment during coliform mastitis in cows within ten days after calving, compared with cows at midlactation. American Journal of Veterinary Research 57 1569–1577CrossRefGoogle ScholarPubMed
Strek, M, Gorlach, S, Podsedek, A, Sosnowska, D, Koziolkiewicz, M, Hrabec, Z & Hrabec, E 2007 Procyanidin oligomers from Japanese quince (Chaenomeles japonica) fruit inhibit activity of MMP-2 and MMP-9 metalloproteinases. Journal of Agricultural and Food Chemistry 55 6447–6452CrossRefGoogle ScholarPubMed
Su, WJ, Chang, CJ, Peh, HC, Lee, SL, Huang, MC & Zhao, X 2002 Apoptosis and oxidative stress of infiltrated neutrophils obtained from mammary glands of goats during various stages of lactation. American Journal of Veterinary Research 63 241–246CrossRefGoogle ScholarPubMed
Tian, SZ, Chang, CJ, Chiang, CC, Peh, HC, Huang, MC, Lee, JW & Zhao, X 2005 Comparison of morphology, viability and function between blood and milk neutrophils from peak lactating goats. Canadian Journal of Veterinary Research 69 39–45Google ScholarPubMed
Visse, R & Nagase, H 2003 Matrix metalloproteinases and tissue inhibitors of metalloproteinases structure, function, and biochemistry. Circulatory Research 92 827–839CrossRefGoogle ScholarPubMed
Weng, MH, Chang, CJ, Chen, YW, Chou, WK, Peh, HC & Huang, MC 2006 Contribution of somatic cell-associated activation of plasminogen to caseinolysis within the goat mammary gland. Journal of Dairy Science 89 2025–2037CrossRefGoogle ScholarPubMed
Wilde, CJ, Knight, CH & Flint, DJ 1999 Control of milk secretion and apoptosis during mammary involution. Journal of Mammary Gland Biology and Neoplasia 4 129–136CrossRefGoogle ScholarPubMed
Xue, M, Thompson, PJ, Clifton-Bligh, R, Fulcher, G, Gallery, EDM & Jackson, C 2005 Leukocyte matrix metalloproteinase-9 is elevated and contributes to lymphocyte activation in type I diabetes. International Journal of Biochemistry and Cell Biology 37 2406–2416CrossRefGoogle ScholarPubMed