Chromosomal localization of lipolytic enzymes in the mouse: pancreatic lipase, colipase, hormone-sensitive lipase, hepatic lipase, and carboxyl ester lipase.

نویسندگان

  • C H Warden
  • R C Davis
  • M Y Yoon
  • D Y Hui
  • K Svenson
  • Y R Xia
  • A Diep
  • K Y He
  • A J Lusis
چکیده

Several lipases and their cofactors are involved in the absorption, transport, storage, and mobilization of lipids. As part of an effort to examine the role of these enzymes in plasma lipid metabolism and genetic susceptibility to atherosclerosis, we report the chromosomal mapping of their genes in mouse. Restriction fragment length variants for each gene were identified, typed in an interspecific cross, and tested for linkage to known chromosomal markers. The gene for pancreatic lipase resides on chromosome 19, while the gene for its cofactor, colipase, is on chromosome 17. A gene for a protein with sequence similarity to pancreatic lipase was tightly linked (no observed recombination) to the gene for pancreatic lipase, suggesting a gene cluster. The gene for hormone-sensitive lipase is near the gene cluster containing apolipoproteins C-II and E on chromosome 7. The gene for hepatic lipase is near the gene for apolipoprotein A-I on chromosome 9. The carboxyl ester lipase gene resides on chromosome 2. Previously, we have mapped the gene for lipoprotein lipase to chromosome 8. Thus, with the exception of pancreatic lipase and a related protein, these lipase genes, including several that are members of a gene family, are widely dispersed in the genome. Comparison of chromosomal locations for these genes in mouse and humans shows that the previously observed interspecies syntenies are preserved.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Studies on the effect of bile and lipolysis products on pancreatic lipase and colipase activity in vitro.

This study shows that human bile, at a concentration in the range of that found in the intestinal lumen, inhibited the hydrolysis of emulsified triolein by pancreatic lipase in vitro. The addition of colipase in excess to lipase failed to restore lipolytic activity. In contrast, a partially degraded emulsion of triolein containing diacylglycerol, monoacylglycerol and free fatty acid was hydroly...

متن کامل

Effects of Pre-clinical Administration of Marshmallow Extract (Althaea officinalis L.) on Certain Hepatopancreatic Enzymes in Common Carp (Cyprinus carpio)

This study evaluates the influence of marshmallow extract administration (Althaea officinalis L.) at 0.0 (control), 2.5, 5, and 10 g on the activity of certain hepatopancreatic enzymes such as α-amylase, lipase and trypsin in common carp (Cyprinus carpio) during 60 days. Feeding the fish with diets enriched with marshmallow extract had no effects on the satiety index and hepatic index in these ...

متن کامل

Principles of Physiology of Lipid Digestion

The processing of dietary lipids can be distinguished in several sequential steps, including their emulsification, hydrolysis and micellization, before they are absorbed by the enterocytes. Emulsification of lipids starts in the stomach and is mediated by physical forces and favoured by the partial lipolysis of the dietary lipids due to the activity of gastric lipase. The process of lipid diges...

متن کامل

Lipase isoforms and amylase isoenzymes: assays and application in the diagnosis of acute pancreatitis.

Pancreatic juice and serum from patients with acute pancreatitis contain three enzymes that have lipolytic activity: L1 and L2, which are pancreatic isoenzymes or isoforms of lipase (EC 3.1.1.3), and L3, which is probably pancreatic carboxyl ester lipase, also known as cholesterol esterase (EC 3.1.1.13). These enzymes are readily separated electrophoretically on agarose and can be developed wit...

متن کامل

Molecular Cloning and Characterization of a Lipase from an Indigenous Bacillus pumilus

Cloning and sequencing of a lipase gene from an indigenous Bacillus pumilus, strain F3, revealed an open-reading frame of 648 nucleotides predicted to encode a protein of 215 residues. Sequence analysis showed that F3 lipase contained a signal peptide composed of 34 amino acids with an H domain of 18 residues. A tat-like motif was found in the signal peptide similar to some other Bacillus pumil...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of lipid research

دوره 34 8  شماره 

صفحات  -

تاریخ انتشار 1993