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Mammary lipoprotein lipase in plasma of cows after parturition or prolactin infusion
Author(s) -
Liesman James S.,
Emery Roy S.,
Akers R. Michael,
Tucker H. Allen
Publication year - 1988
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02535528
Subject(s) - prolactin , medicine , endocrinology , lipoprotein lipase , lipase , mammary gland , umbilical vein , lactation , chemistry , blood plasma , triacylglycerol lipase , biology , hormone , enzyme , pregnancy , adipose tissue , biochemistry , in vitro , genetics , cancer , breast cancer
Plasma lipase activity from the mammary vein and a tail blood vessel was measured in periparturient Holstein cows treated in one of three ways: control, CB154 (2‐Br‐α‐ergocryptin) or CB154 plus prolactin. CB154 administration decreased basal serum prolactin concentration by 80% and blocked the normal parturient increase of serum prolactin. In CB154 plus prolactin‐treated cows, prolactin was infused continously for six days starting five and eight days prepartum. Plasma lipase activity was not detectable up to 26 hr prepartum in control and CB154‐treated cows or before the start of prolactin infusion in CB154 plus prolactin‐treated cows. After two hr prepartum, plasma lipase activity was detected in all treatments. In CB154 plus prolactin‐treated cows, plasma lipase activity was detected in the presence of high concentrations of serum progesterone four days after the start of prolactin infusion and at least two days before parturition. Plasma lipase activity was four times greater in the mammary vein than in the tail vessel at sampling times at which activity was detected in both vessels. We propose the difference between plasma lipase activity from the mammary vein and tail vessel is due to release of lipoprotein lipase from the mammary gland into blood, and this activity can be induced prepartum by prolactin or at parturition even if the parturient increase in prolactin is suppressed.