RESUMEN
PURPOSE: To determine the structure, location, and tissue-specific expression of the mouse opticin gene (Optc) and to compare expression in the eye with that of Prelp, collagen II, and collagen IX. METHODS: Expressed sequence tags (ESTs) to mouse opticin were identified and the full-length sequence obtained after PCR reactions using a 15-day-postconception (dpc) whole-mouse embryo cDNA library. The mouse chromosomal localization of Optc was determined by radiation hybrid mapping and its genomic structure determined using an Optc-containing BAC clone. Tissue-specific expression of opticin, PRELP, collagen II, and collagen IX mRNAs was investigated by in situ hybridization and by dot blot hybridization for opticin. RESULTS: The Optc gene was localized to mouse chromosome 1 at 74.3 cM and consisted of seven exons spanning 10 kb. The Optc gene was less than 4 kb from the Prelp gene. In situ hybridization localized opticin mRNA exclusively to the presumptive ciliary body during development and to the nonpigmented ciliary epithelium of the adult mouse eye. Expression of Prelp was also detected in the nonpigmented ciliary epithelium of the adult eye. However, expression of collagen types II and IX was detected largely in the developing mouse eye, with type IX expression confined primarily to the presumptive ciliary body. CONCLUSIONS: The Optc, Prelp, and fibromodulin (Fmod) genes form a cluster on mouse chromosome 1. Opticin may represent a marker for ciliary body differentiation. Continued expression of opticin in the adult mouse eye suggests functions other than that of putative regulator of vitreous collagen fibrillogenesis.
Asunto(s)
Mapeo Cromosómico , Cromosomas/genética , Cuerpo Ciliar/metabolismo , Proteínas de la Matriz Extracelular/genética , Proteínas del Ojo/genética , Proteoglicanos/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Cuerpo Ciliar/embriología , Colágeno/genética , Colágeno/metabolismo , Etiquetas de Secuencia Expresada , Proteínas de la Matriz Extracelular/metabolismo , Proteínas del Ojo/metabolismo , Expresión Génica , Glicoproteínas/genética , Glicoproteínas/metabolismo , Humanos , Hibridación in Situ , Ratones , Ratones Endogámicos BALB C , Datos de Secuencia Molecular , Reacción en Cadena de la Polimerasa , Proteoglicanos/metabolismo , ARN Mensajero/metabolismo , Homología de Secuencia de Aminoácido , Homología de Secuencia de Ácido NucleicoRESUMEN
We have discovered a new member of the class I small leucine-rich repeat proteoglycan (SLRP) family which is distinct from the other class I SLRPs since it possesses a unique stretch of aspartate residues at its N terminus. For this reason, we called the molecule asporin. The deduced amino acid sequence is about 50% identical (and 70% similar) to decorin and biglycan. However, asporin does not contain a serine/glycine dipeptide sequence required for the assembly of O-linked glycosaminoglycans and is probably not a proteoglycan. The tissue expression of asporin partially overlaps with the expression of decorin and biglycan. During mouse embryonic development, asporin mRNA expression was detected primarily in the skeleton and other specialized connective tissues; very little asporin message was detected in the major parenchymal organs. The mouse asporin gene structure is similar to that of biglycan and decorin with 8 exons. The asporin gene is localized to human chromosome 9q22-9q21.3 where asporin is part of a SLRP gene cluster that includes extracellular matrix protein 2, osteoadherin, and osteoglycin. Further analysis shows that, with the exception of biglycan, all known SLRP genes reside in three gene clusters.
Asunto(s)
Expresión Génica , Glicoproteínas/genética , Leucina/química , Proteínas/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Proteínas Portadoras , Mapeo Cromosómico , Cromosomas Humanos Par 9 , ADN Complementario , Proteínas de la Matriz Extracelular , Glicoproteínas/química , Humanos , Proteínas Repetidas Ricas en Leucina , Ratones , Datos de Secuencia Molecular , Proteínas/química , Homología de Secuencia de AminoácidoRESUMEN
1. That the cholesterol content of the whole blood taken the population in and around Calcutta must be considered as slightly lower than the usually acceoted european and American figure.2. That he cholesterol content of the blood of lepers is reduced in the early stages of the disease.3. That in advanced skin cases the content is much more reduced.4. That in advanced treatment cases the blood cholesterol content does not return to normal.5. That anti-rabic treatment has no effect on the cholesterol content of whole blood.The expense of this work has been defrayed from a grant received from the Indian Research Fund Association.