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Tissue-type plasminogen activator and plasminogen embedded in casein rule its degradation under physiological situations: Manipulation with casein hydrolysate
Year:
2013
Source of publication :
Journal of Dairy Research
Authors :
Merin, Uzi
;
.
Shapiro, Fira
;
.
Silanikove, Nissim
;
.
Volume :
80
Co-Authors:
Silanikove, N., Biology of Lactation Laboratory, Institute of Animal Science, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Shapiro, F., Biology of Lactation Laboratory, Institute of Animal Science, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Merin, U., Department of Food Quality and Safety, Institute of Postharvest and Food Sciences, Volcani Center, P.O. Box. 6, Bet Dagan 50250, Israel
Leitner, G., National Mastitis Reference Center, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel
Facilitators :
From page:
227
To page:
232
(
Total pages:
6
)
Abstract:
The aims of this study were to test the assumption that tissue-type plasminogen activator (t-PA) and plasminogen (PG) are closely associated with the casein micelle and form a functional complex that rules casein degradation. This assumption was essentially verified for bovine milk under conditions wherein the plasmin system was activated by treatment with casein hydrolysate. It was also shown that urokinase-type PA (u-PA), the second type of plasminogen activator present in milk, was not involved in casein degradation. In agreement with previous studies, we show that treatment with casein hydrolysate precipitously reduced mammary secretion, disrupted the tight junction integrity (increase in Na+ and decrease in K+ concentrations), induced hydrolysis of casein, and activated various elements of the innate and acquired immune system. In the present study, we have identified t-PA as the principal PA, which is responsible for the conversion of PG to plasmin. It was found that t-PA and plasminogen are present in freshly secreted milk (less than 10Â min from its secretion), suggesting that they are secreted as a complex by the mammary gland epithelial cells. Further research is needed to provide the direct evidence to verify this concept. Copyright © Proprietors of Journal of Dairy Research 2013.
Note:
Related Files :
Animal
Animals
casein
Caseins
cattle
chemistry
Female
metabolism
milk
plasmin
Urokinase-type plasminogen activator
Show More
Related Content
More details
DOI :
10.1017/S0022029913000010
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
25637
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:16
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Scientific Publication
Tissue-type plasminogen activator and plasminogen embedded in casein rule its degradation under physiological situations: Manipulation with casein hydrolysate
80
Silanikove, N., Biology of Lactation Laboratory, Institute of Animal Science, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Shapiro, F., Biology of Lactation Laboratory, Institute of Animal Science, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel
Merin, U., Department of Food Quality and Safety, Institute of Postharvest and Food Sciences, Volcani Center, P.O. Box. 6, Bet Dagan 50250, Israel
Leitner, G., National Mastitis Reference Center, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel
Tissue-type plasminogen activator and plasminogen embedded in casein rule its degradation under physiological situations: Manipulation with casein hydrolysate
The aims of this study were to test the assumption that tissue-type plasminogen activator (t-PA) and plasminogen (PG) are closely associated with the casein micelle and form a functional complex that rules casein degradation. This assumption was essentially verified for bovine milk under conditions wherein the plasmin system was activated by treatment with casein hydrolysate. It was also shown that urokinase-type PA (u-PA), the second type of plasminogen activator present in milk, was not involved in casein degradation. In agreement with previous studies, we show that treatment with casein hydrolysate precipitously reduced mammary secretion, disrupted the tight junction integrity (increase in Na+ and decrease in K+ concentrations), induced hydrolysis of casein, and activated various elements of the innate and acquired immune system. In the present study, we have identified t-PA as the principal PA, which is responsible for the conversion of PG to plasmin. It was found that t-PA and plasminogen are present in freshly secreted milk (less than 10Â min from its secretion), suggesting that they are secreted as a complex by the mammary gland epithelial cells. Further research is needed to provide the direct evidence to verify this concept. Copyright © Proprietors of Journal of Dairy Research 2013.
Scientific Publication
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