title: Cloning and regulation of cornifin beta, a new member of the cornifin/spr family. Suppression by retinoic acid receptor-selective retinoids.
abstract: In this study, we describe the isolation and characterization of a cDNA clone C12 that encodes a new member of the cornifin/small proline-rich protein (spr) family, which we have named cornifin beta. C12 encodes a 1.1-kilobase pair mRNA and a 24.3-kDa cytosolic protein with a high proline content (19%). Its total amino acid sequence exhibits a 37-66% identity while the first 30 amino acids at the amino terminus are 87% identical to that of members of the cornifin family. At its carboxyl terminus, cornifin beta contains 21 tandem repeats of an octapeptide. Cornifin beta expression is restricted to several squamous epithelia. It is highly expressed in esophagus, tongue, and oral mucosa but, in contrast to cornifin alpha, is not detectable in the epidermis. Both retinoic acid and a retinoid selective for the nuclear retinoic acid receptors were very potent suppressors of cornifin beta expression while an analog selective for the nuclear retinoid X receptors was much less effective, suggesting that a specific retinoid signaling pathway is involved in this suppression. Cornifin beta can function through some of its Gln residues as an amine acceptor in transglutaminase-catalyzed cross-linking reactions. These results indicate that cornifin beta functions as a cross-linked envelope precursor.
authors.affiliation: Cell Biology Section, Laboratory of Pulmonary Pathobiology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA.
authors.forename: S J
authors.initials: SJ
authors.lastname: Austin
authors.forename: W
authors.initials: W
authors.lastname: Fujimoto
authors.forename: K W
authors.initials: KW
authors.lastname: Marvin
authors.forename: T M
authors.initials: TM
authors.lastname: Vollberg
authors.forename: L
authors.initials: L
authors.lastname: Lorand
authors.forename: A M
authors.initials: AM
authors.lastname: Jetten
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002454:Cell Differentiation; D002478:Cells, Cultured; D003001:Cloning, Molecular; D055233:Cornified Envelope Proline-Rich Proteins; D003600:Cytosol / Q000378:metabolism; D004848:Epithelium; D004947:Esophagus / Q000166:cytology / Q000378:metabolism; D015870:Gene Expression / Q000187:drug effects*; D015723:Gene Library; D005973:Glutamine; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D008046:Lip / Q000166:cytology / Q000378:metabolism; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010455:Peptides / Q000737:chemistry; D055232:Proline-Rich Protein Domains; D014176:Protein Biosynthesis; D011506:Proteins / Q000032:analysis / Q000737:chemistry; D012333:RNA, Messenger / Q000378:metabolism; D011817:Rabbits; D018168:Receptors, Retinoic Acid / Q000037:antagonists & inhibitors*; D047488:Retinoid X Receptors; D012176:Retinoids / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D014059:Tongue / Q000166:cytology / Q000378:metabolism; D014132:Trachea; D014157:Transcription Factors / Q000037:antagonists & inhibitors; D011503:Transglutaminases / Q000378:metabolism
chemical_list: D055233:Cornified Envelope Proline-Rich Proteins; D010455:Peptides; D011506:Proteins; D012333:RNA, Messenger; D018168:Receptors, Retinoic Acid; D047488:Retinoid X Receptors; D012176:Retinoids; D014157:Transcription Factors; D005973:Glutamine; D011503:Transglutaminases