Immunoelectron microscopic localization of fibronectin in the smooth muscle layer of mouse small intestine.
Author(s) -
Kojiro Kurisu,
Yasuyoshi Ohsaki,
K. Nagata,
T Kukita,
Hiroshi Yoshikawa,
Tetsuichiro Inai
Publication year - 1987
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/35.4.3546487
Subject(s) - fibronectin , basal lamina , immunogold labelling , extracellular matrix , basement membrane , lamina lucida , lamina densa , microbiology and biotechnology , endoplasmic reticulum , biology , immunoelectron microscopy , matrix (chemical analysis) , extracellular , chemistry , biophysics , ultrastructure , laminin , anatomy , antibody , immunology , chromatography
We studied the ultrastructural distribution of fibronectin in the smooth muscle layer of mouse small intestine with affinity-purified antibodies using the immunogold technique. Fibronectin was present over the pericellular area extending from the cell membrane to the extracellular matrix beyond the basal lamina. Distribution of the glycoprotein over the pericellular area was heterogeneous, i.e., it was localized more abundantly in the narrow space between smooth muscle cells, the gaps having a width of 60-80 nm where the two dense bands in adjacent cells matched each other. Such localization suggests that fibronectin contributes to cell adhesion. Within the basement membrane, gold label was localized both in lamina lucida and lamina densa, more densely in the latter than in the former. Fibronectin was also co-distributed with collagen fibers in the extracellular matrix. Within smooth muscle cells, gold particles were observed on rough endoplasmic reticulum and secretory vesicle-like structures. These results suggest that smooth muscle cells synthesize fibronectin and secrete it as a component of the basal lamina and extracellular matrix.
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