Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development

R. M. Payne, H. F. Sims, M. L. Jennens, M. E. Lowe

Research output: Contribution to journalArticle

94 Scopus citations

Abstract

We report the cDNA sequences of rat colipase, rat pancreatic lipase (rPL), and a rat pancreatic lipase-related protein (rPLRP). Comparison to the human PLRP cDNA suggests that the isolated clone encodes rPLRP-2. Both cDNA and a third cDNA encoding rPLRP-1 are secreted from Sf9 cells infected with recombinant baculovirus. rPL and rPLRP-2 hydrolyze triolein, 8.0 and 4.4 μmol · min-1 · μg-1, respectively. They are inhibited by bile salts, and activity is restored by (pro)colipase. PLRP-1 has barely detectable activity against triolein, even with (pro)colipase present. The pattern of mRNA expression during development in the rat reveals that all mRNA are low in the fetal rat pancreas. Both PLRP mRNA rise just before birth to a maximum 12 h after birth. They fall to low levels in the adult. In contrast, the PL mRNA is low at birth and rises rapidly during the suckling-veanling transition. In conclusion, the rat has at least three genes encoding different lipases, and these related genes have separate regulatory controls.

Original languageEnglish (US)
Pages (from-to)G914-G921
JournalAmerican Journal of Physiology - Gastrointestinal and Liver Physiology
Volume266
Issue number5 29-5
DOIs
StatePublished - 1994
Externally publishedYes

Keywords

  • baculovirus
  • protein expression
  • triglycerides

ASJC Scopus subject areas

  • Physiology
  • Hepatology
  • Gastroenterology
  • Physiology (medical)

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