Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1993-9-24
pubmed:abstractText
The human insulin receptor exists in two isoforms (HIR-A alpha-subunit 719 amino acids and HIR-B alpha-subunit 731 amino acids) which are generated by alternative splicing of a small exon and display distinct patterns of tissue-specific expression. Using the polymerase chain reaction we have recently shown that skeletal muscle of non-diabetic individuals contains predominantly mRNA encoding HIR-A while in skeletal muscle derived from subjects with Type 2 (non-insulin-dependent) diabetes mellitus similar amounts of each mRNA are expressed. We used a polyclonal antibody which discriminates between HIR-A and HIR-B to assess the isoform expression at the protein level. The antibody showed clearly distinct displacement of insulin binding in skeletal muscle membranes of non-diabetic subjects compared to Type 2 diabetic subjects (displacement of specific 125I-insulin binding: 13 non-diabetic subjects 70.0% +/- 14.34, 12 Type 2 diabetic subjects 32.6% +/- 17.45). A control antibody which does not discriminate between both isoforms showed similar displacement of 125I-insulin in membranes of non-diabetic and Type 2 diabetic subjects. These data suggest that the altered expression of receptor isotype mRNA in the skeletal muscle of Type 2 diabetic subjects leads to an altered receptor isoform pattern in the plasma membrane. While skeletal muscle membranes of non-diabetic subjects contain predominantly HIR-A, membranes of Type 2 diabetic subjects show an increased level of HIR-B in addition to HIR-A.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0012-186X
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
628-32
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:8359580-Aged, pubmed-meshheading:8359580-Aged, 80 and over, pubmed-meshheading:8359580-Alternative Splicing, pubmed-meshheading:8359580-Animals, pubmed-meshheading:8359580-Blood Glucose, pubmed-meshheading:8359580-Cell Line, pubmed-meshheading:8359580-Diabetes Mellitus, Type 2, pubmed-meshheading:8359580-Hemoglobin A, Glycosylated, pubmed-meshheading:8359580-Humans, pubmed-meshheading:8359580-Insulin, pubmed-meshheading:8359580-Kinetics, pubmed-meshheading:8359580-L-Lactate Dehydrogenase, pubmed-meshheading:8359580-Macromolecular Substances, pubmed-meshheading:8359580-Middle Aged, pubmed-meshheading:8359580-Muscles, pubmed-meshheading:8359580-Phosphofructokinase-1, pubmed-meshheading:8359580-Phosphoglucomutase, pubmed-meshheading:8359580-Phosphoglycerate Kinase, pubmed-meshheading:8359580-RNA, Messenger, pubmed-meshheading:8359580-Rats, pubmed-meshheading:8359580-Receptor, Insulin, pubmed-meshheading:8359580-Reference Values, pubmed-meshheading:8359580-Transfection
pubmed:year
1993
pubmed:articleTitle
Altered pattern of insulin receptor isotypes in skeletal muscle membranes of type 2 (non-insulin-dependent) diabetic subjects.
pubmed:affiliation
Institut für Diabetesforschung, Munich, Germany.
pubmed:publicationType
Journal Article