Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-19
pubmed:databankReference
pubmed:abstractText
Myocilin is known to be associated with the pathogenesis of juvenile-onset primary open angle glaucoma. The tissue distribution of myocilin transcripts has been analyzed in both humans and mice, and a high level of expression in the retina and skeletal muscle has been reported. The functions of myocilin in these tissues are unknown. We isolated rat myocilin cDNA and examined the expression pattern of myocilin, including its expression in endocrine organs, using Northern blot analysis. The rat myocilin cDNA sequence has two in-frame initiation codons, the upstream and downstream ATGs corresponding to the initiation codon of human and murine myocilin, respectively. It is most likely that the first ATG is a translational initiation codon, since 8 of 13 amino acid residues deduced from the rat cDNA sequence between the first and the second ATGs are the same as those in human myocilin. The open reading frame encodes 502 amino acids. Rat myocilin also has both a myosin-like domain and an olfactmedin-like domain, which have been identified in human and murine myocilin. Northern analysis of rat myocilin mRNA revealed substantial expression in the thyroid gland, as well as in the retina and muscle. No transcripts were detected in other endocrine glands, including the adrenal gland, pituitary, and testis. Myocilin may play an important role in thyroid function. Further study of the expression and role of myocilin in the thyroid is required.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1096-7192
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10833334-Amino Acid Sequence, pubmed-meshheading:10833334-Animals, pubmed-meshheading:10833334-Base Sequence, pubmed-meshheading:10833334-Blotting, Northern, pubmed-meshheading:10833334-Cloning, Molecular, pubmed-meshheading:10833334-Cytoskeletal Proteins, pubmed-meshheading:10833334-DNA, Complementary, pubmed-meshheading:10833334-Eye Proteins, pubmed-meshheading:10833334-Gene Expression Profiling, pubmed-meshheading:10833334-Glycoproteins, pubmed-meshheading:10833334-Male, pubmed-meshheading:10833334-Molecular Sequence Data, pubmed-meshheading:10833334-Muscle, Skeletal, pubmed-meshheading:10833334-RNA, Messenger, pubmed-meshheading:10833334-Rats, pubmed-meshheading:10833334-Rats, Wistar, pubmed-meshheading:10833334-Retina, pubmed-meshheading:10833334-Sequence Alignment, pubmed-meshheading:10833334-Sequence Analysis, DNA, pubmed-meshheading:10833334-Sequence Homology, Amino Acid, pubmed-meshheading:10833334-Thyroid Gland, pubmed-meshheading:10833334-Tissue Distribution
pubmed:year
2000
pubmed:articleTitle
Molecular cloning and expression profile of rat myocilin.
pubmed:affiliation
Department of Endocrinology and Metabolism, Toranomon Hospital, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't