Abstract. The fine distribution of the extracellular matrix glycoprotein emilin (previously known as glycoprotein gp115) (Bressan, G. M., I. Castellani, A. Colombatti, and D. Volpin. 1983. J. Biol. Chem. 258: 13262-13267) has been studied at the ultrastructural level with specific antibodies. In newborn chick aorta the protein was exclusively found within elastic fibers. In both post-and pre-embedding immunolabeling emilin was mainly associated with regions where elastin and microfibrils are in close contact, such as the periphery of the fibers. This localization of emilin in aorta has been confirmed by quantitative evaluation of the distribution of gold particles within elastic fibers. In other tissues, besides being associated with typical elastic fibers, staining for emilin was found in structures lacking amorphous elastin, but where the presence of tropoelastin has been demonstrated by immunoelectron microscopy. This was particularly evident in the oxitalan fibers of the corneal stroma, in the Descemet's membrane, and in the ciliary zonule. Analysis of embryonic aorta revealed the presence of emilin at early stages of elastogenesis, before the appearance of amorphous elastin. Immunofluorescence studies have shown that emilin produced by chick embryo aorta cells in culture is strictly associated with elastin and that the process of elastin deposition is severely altered by the presence of antiemilin antibodies in the culture medium. The name of the protein was derived from its localization at sites where elastin and microfibrils are in proximity (emilin, elastin microfibril interface located protein).

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Histological and chemical studies were carried out on the elastin and collagen content of the normal and the obstructed urinary bladder wall. The observations were made on 3 different age groups: (1) 3-month-old children with vesical outlet obstruction, (2) children aged between 4 and 8 years with partial vesical obstruction, and (3) adults with a chronically obstructed bladder. An increase in elastic tissue was shown only in the newborn and in the adults. The collagen did not vary in any of the cases studied. The elastin showed an increase in polar amino acids in the pathological organs compared with the normal. A similar increase in elastin was observed in normal individuals as a result of the ageing process.

An extracellular glycoprotein (gp 115) with an apparent Mr = 115,000 isolated from chick aortas (Bressan, G. M., i. Castellani, A. Colombatti, and D. Volpin, 1983, J. Biol. Chem., 258:13262-13267), was used to immunize mice. The antisera were shown to specifically recognize gp 115 by numerous criteria: a major band around Mr = 115,000 plus minor bands of lower Mr were visible by immunoblotting on aorta extracts, and a similar pattern was observed with a monoclonal antibody; no cross-reactivity was detected by radioimmunobinding with other extracellular proteins, namely, fibronectin, laminin, and collagen types I, III, IV, V, and Vl. Antigen distribution on frozen tissue sections from newborn chicks was investigated by using affinity-purified antibody. Strong immunoreactivity was always found in blood vessels. In the digestive tract, the fluorescent staining was localized both at the level of muscular layers and in the stromal matrix of the villi. Within skeletal muscle and myocardium, staining was associated with large connective tissue bundles and the matrix around each muscle fiber. Intense fluorescence was observed in the kidney, in smooth muscle cells rich areas of parabronchi, and within the portal space and along liver sinusoids. The antigen was not detected at the epidermal-dermal junction; immunoreactivity in the dermis was present as a diffuse fibrillar pattern. That the antigen detected by immunofluorescence in the various organs was indeed gp 115 was demonstrated by immunoblotting analysis: as in aorta extracts, a major band around Mr --115,000 was detected in several tissues. Antibody-reacting material was also incorporated into the extracellular matrix produced by embryo smooth muscle cells grown in vitro and was organized as a meshwork of fine fibrils.There is increasing evidence suggesting that the extracellular matrix plays an important role in establishing and organizing tissue structure (I, 2). This is likely to be the result of multiple interactions between cells and a specific set of extracellular components in the different anatomical districts. The knowledge of tissue distribution of each novel molecular species is the first step toward the understanding of its possible function. Thus, a characteristic pattern of distribution has been detected in the various organs for several components of the connective tissue such as the different collagen types (3, 4), fibronectin (5, 6), laminin (7), entactin (8), vitronectin (9), and proteoglycans (10, 11). In addition, the composition of the matrix is closely dependent on the cell type and the degree of its differentiation (2).While studying the proteins of chick blood vessels, we have identified a noncollagenous glycoprotein of about Mr = l 15,000 (gp 115), which was unrelated by biochemical and immunological criteria to the major known extracellular glycoproteins, fibronectin and laminin (12).The investigation of the distribution of gp 115 in tissues t?om newborn chicks by using immunofluorescence histochemistry is reported here. We have ...