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Query: UNIPROT:Q9UIJ5 (
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58,342
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The anatomical structure as well as the smooth muscle cell (SMC1) composition of the ductus arteriosus (DA) were studied in rabbits ranging in age from 29 days of gestation to 20 days after birth. Computer-assisted, three-dimensional reconstructions of hematoxylin-eosin stained serial cryosections from ductus arteriosus-aorta (DA-AO) junctures revealed that DA in animals near term is separated from the aorta by a "septumlike" structure that is continuous with the aortic wall. Two days after birth, obliteration of DA is almost complete, and a small "pocketlike" cavity appears in the pre-existing site in which DA merged into the aorta. This small cavity in the aortic arch was still evident in the large majority of animals examined even 20 days after birth, as also demonstrated by scanning electron microscopy. At this time period DA consisted of a central, fibrotic region surrounded by several layers of SMC (the ligamentum arteriosum, LA) and ended within the aortic media just above the small cavity, forming a round "scar." Vascular SMC composition of DA during closure was examined by means of indirect and double immunofluorescence procedures, using a panel of monoclonal antibodies against some cytoskeletal and cytocontractile proteins (
vimentin
, desmin, smooth muscle (SM), and nonmuscle (NM) myosin isoforms). "Intimal cushions" were particularly evident from 5 hr after birth and were found to be desmin-negative, homogenously reactive for
vimentin
and NM myosin, and heterogeneously stained with anti-SM myosin antibody. In SMC subjacent to the "intimal cushions," distribution of
vimentin
and SM myosin was homogeneous, whereas the one of desmin and NM myosin content was heterogeneous. The cytoskeletal and cytocontractile protein content displayed by SMC during the closure of DA is similar to that of "intimal thickening" found in some pathological conditions of the arterial wall in adult rabbits. Completation of DA closure (day 2) was accompanied by the disappearance of cellular heterogeneity in myosin isoform distribution in both the "intimal cushions" and the underlying media. These results give new insights into: (1) the structure of DA-AO juncture, which can be relevant to the physiology of blood circulation in the fetus, and (2) the phenotypic similarity of vascular SMC populations involved in the formation of "intimal cushions" and "intimal thickening."
Anat
Rec
1993 Jan
PMID:Rabbit ductus arteriosus during development: anatomical structure and smooth muscle cell composition. 841 32
We have developed a co-culture system suited for the study of epithelial-mesenchymal interactions in the human fetal small intestine. As the epithelial component of this model, we used the human intestinal cell line Caco-2 that is unique in its property to differentiate in vitro into a mature fetal enterocyte-like cell type. A sheet of human intestinal mesenchymal cells, which we derived from an 18-week-old fetus, was used as mesenchymal element. Expression and distribution of cell-specific markers (cytokeratin 18 and dipeptidyl peptidase IV), major basement membrane components, and beta 1 integrins were analyzed. In 14-day co-cultures, Caco-2 cells formed a cytokeratin 18-positive epithelial-like sheet covering the
vimentin
-positive HIM cell layers. As assessed by brush border dipeptidyl peptidase IV expression, co-cultured Caco-2 cells achieved cytodifferentiation as when cultured on plastic. A complete deposition of all known major human fetal intestinal basement membrane components occurred at the Caco-2/HIM interface. Type IV collagen and tenascin were produced from the mesenchymal compartment, whereas laminin and fibronectin were contributed by both cell types. Interestingly, synthesis and deposition of basement membrane heparan sulfate proteoglycan were exclusively observed in co-cultures, suggesting modulation of epithelial expression of this molecule by HIM cells. Finally, we observed that epithelial integrin-beta 1 chains redistributed at the basal domain of co-cultured Caco-2 cells. Taken together, these observations indicate that the Caco-2/HIM co-culture model is a valuable system to study in vitro human basement membrane formation in the context of intestinal epithelial-mesenchymal interactions.
Anat
Rec
1993 Apr
PMID:Basement membrane formation and re-distribution of the beta 1 integrins in a human intestinal co-culture system. 846 88
A five-year-old female red deer (Cervus elaphus) was in poor condition and severely lame on the left hindleg owing to a 19.4 cm x 15.9 cm mass involving and destroying the distal end (head) of metatarsal bones III and IV, the proximal sesamoid bones and the first phalanges (III and IV). The histopathological analysis revealed a spindle cell tumour with frequent palisade arrangement (Antoni type A pattern), and with highly anaplastic tumour cells in some areas. Structures resembling peripheral nerves were identified within the tumour. The neoplastic cells reacted with
vimentin
in a cytoplasmic pattern, and almost all of them reacted with S-100 protein in a nuclear and cytoplasmic pattern and did not express neurofilament, glial fibrillary acidic protein or keratins. This immunophenotype and the histopathological features were consistent with a diagnostic of malignant schwannoma. It was atypical because of the species affected, the location and the local malignancy.
Vet
Rec
1998 Nov 21
PMID:Malignant schwannoma in a red deer (Cervus elaphus). 985 70
The purpose of the present study was to investigate the pattern of distribution of cytokeratins,
vimentin
and muscular actin in the testis of vicuna (Vicugna vicugna) and llama (Lama glama) two species of camelids native of the Andean high plateau of South America. Testicular biopsies of four vicunas and five llamas were used. Animals were healthy breeders. The tissues were processed by standard immunohistochemistry with antipancytokeratinAE1/AE3, antikeratin 18 (K 18), CAM 5.2 (antikeratin 5, 18, and 19), antivimentin, and smooth-muscle-specific antiactin antibodies to track the cytoskeletal pattern of testicular cells. Using AE1/AE3 antibody the immunostaining was found in the epithelial lining of tubuli recti and rete testis. The reaction was relatively stronger in the apical cytoplasm of epithelial cells. The testicular cells of the two species showed no reaction to K 18 and CAM 5.2 antibodies. Antivimentin antibody stained the basal cytoplasm of the Sertoli cells, the Leydig cells, and the epithelial lining of tubuli recti and rete testis. In the last two structures the immunostain was relatively more intense in the basal cytoplasm of epithelial cells. Antiactin antibody stained the peritubular cells and the muscle cells of the lamina propria oftubuli recti and rete testis. The presence in these species of only some keratins found in man, its coexpression with
vimentin
in epithelial lining of tubuli recti and rete testis and the peritubule organization, so different from other ungulates may reflect a differential adaptation of the cytoskeleton to particular reproductive strategies.
Anat
Rec
1999 03
PMID:Distribution of keratins, vimentin, and actin in the testis of two South American camelids: vicuna (Vicugna vicugna) and llama (Lama glama). An immunohistochemical study. 1009 64
Intermediate filaments in Sertoli cells have a well-defined pattern of distribution. They form a basally situated perinuclear network from which filaments extend peripherally to adhesion plaques at the plasma membrane and to sites of codistribution with other major elements of the cytoskeleton, particularly with microtubules. Although the general pattern of intermediate filament distribution is known, the molecular components involved with linking the filaments to organelles and attachment plaques in these cells have not been identified. One candidate for such a linking element is plectin. In this study we test for the presence of, and determine the distribution of, plectin in Sertoli cells of the rat testis. Fixed frozen sections and fixed epithelial fragments of rat testis were probed for plectin and
vimentin
using antibodies. Tissue was evaluated using standard fluorescence microscopy and confocal microscopy. Plectin in Sertoli cells was concentrated in a narrow zone surrounding the nucleus, and at focal sites, presumably desmosome-like plaques, at interfaces with adjacent cells. Plectin was also concentrated at sites where intermediate filament bundles project into specialized actin-filament containing plaques at sites of attachment to elongate spermatids. Plectin in Sertoli cells is concentrated at the nuclear surface and in junction plaques associated with the plasma membrane. The pattern of distribution is consistent with plectin being involved with linking intermediate filaments centrally (basally) to the nucleus and peripherally to intercellular attachment sites.
Anat
Rec
1999 03
PMID:Plectin is concentrated at intercellular junctions and at the nuclear surface in morphologically differentiated rat Sertoli cells. 1009 74
The development of Meissner-like and Pacinian corpuscles was studied in mice [from postnatal day (Pd) 0 to 42] by using immunohistochemistry for specific corpuscular constituents. The battery of antigens investigated included PGP 9.5 protein and neurofilaments, as markers for the central axon; S100 protein,
vimentin
, and p75(LNGFR) protein, to show Schwann-related cells; and epithelial membrane antigen to identify perineurial-related cells. In Meissner-like corpuscles immunoreactivity (IR) for neuronal markers was found by Pd7 and later. The lamellar cells of these corpuscles expressed first S100 protein IR (Pd7 to Pd42), then
vimentin
IR (Pd12 to Pd42), and transitory p75(LNGFR) IR (Pd7 to Pd19-20). Vimentin IR, but not epithelial membrane antigen, was detected in the capsule-like cells of the Meissner-like corpuscles. On the other hand, the density of Meissner-like corpuscles progressively increased from Pd0 to Pd19-20. Pacinian corpuscles were identified by Pd7. From this time to Pd42 the central axon showed IR for neuronal markers, and the inner core cells were immunoreactive for S100 protein. Moreover,
vimentin
IR was detected in the inner core cells by Pd19 and later. Unexpectedly, the central axons displayed S100 protein IR (from Pd7 to P28), while p75(LNGFR) protein IR or epithelial membrane antigen IR were never detected. Taken together, and based on the expression of the assessed antigens alone, the present results suggest that the Meissner-like and the Pacinian corpuscles in mice become mature around Pd19-Pd28 and Pd20, respectively. Furthermore, these results provide a baseline timetable for future studies in the normal or altered development of sensory corpuscles in mice since specific sensory corpuscles are functionally associated with different subtypes of sensory neurons the development of which is selectively disturbed in genetically manipulated mice.
Anat
Rec
2000 03 01
PMID:Development of Meissner-like and Pacinian sensory corpuscles in the mouse demonstrated with specific markers for corpuscular constituents. 1070 43
In this study, the presence of cells in the intimal region of normal adult bovine pulmonary artery (BPA) was examined by analysis of longitudinal sections at the level of light and transmission electron microscopy. In addition, the morphological and immunohistochemical phenotype of these cells as well as the presence of particular extracellular matrix (ECM) components in this region were also determined. Since ECM production and cell proliferation have been demonstrated to be regulated by locally released growth factors such as transforming growth factor beta (TGFbeta), the presence of TGFbeta-1 in this region was also investigated. Our findings reveal the presence of immature or "nonmuscle" cells into the subendothelial space of normal adult BPA. These cells were characterized by the presence of abundant cytoplasmic organelles and scanty microfilaments. Such cells were negative to antibodies against smooth muscle alpha actin (SM alpha-actin), 1E12, and vWf, but not to
vimentin
. Similar cells have recently been detected in normal adult BPA and canine carotid arteries, but in the medial region. Because of their location in these elastic arteries, the nonmuscle cells are involved not only in the remodeling of the medial region, but also in the neointima or intimal thickening formation by migration from the media to the subendothelial space, where they proliferate and secrete ECM components. However, a limited number of morphological studies and the current investigation describe the presence of scattered nonmuscle cells within the intima of some normal elastic arteries. This would suggest an important role for these resident cells within the intima in normal and pathological processes as well. In addition, our results show the presence, in this region, of TGFbeta-1 and of ECM components that include collagen, elastin, fibronectin, and laminin which are present in normal conditions and during the intima formation in vivo.
Anat
Rec
2000 03 01
PMID:Characterization of nonmuscle cells present in the intima of normal adult bovine pulmonary artery. 1070 46
The lateral wall of the dog cochlear duct was investigated by classical staining and immunohistochemistry for NaK/ATPase beta2 isoform, cytokeratins (Cks),
vimentin
, nestin, and S100A6 during the postnatal cochlear maturation, i.e., from birth to postnatal day 110. The dog stria vascularis was immature at birth. Fine melanin granules were evident in the stria from the second week of life, and melanin concentration increased drastically beyond the first month. The marginal cells were NaK/ATPase- and Ck-positive; intermediate cells were either nestin- and S100A6-positive or
vimentin
-positive; the basal cells were
vimentin
-positive; the capillary endothelium showed
vimentin
and nestin labeling; the cell layer underlying the stria was nestin-positive. The fibrocytes of the spiral ligament and spiral prominence expressed nestin and
vimentin
. The epithelial cells overlaying the spiral prominence and the external sulcus were Ck-positive, and transiently nestin- and
vimentin
-positive. Double immunolabeling, for S100A6 and either nestin,
vimentin
, or NaK/ATPase, and for nestin and
vimentin
suggested the presence of two distinct intermediate cell types. The results enabled us to differentiate the cell types forming the lateral wall of the dog cochlear duct, and to follow their postnatal maturation. This study may form a basis for future investigations about spontaneous cochleosaccular degeneration in dogs. This species is an important companion animal, and a possible model for the study of comparable diseases in humans.
Anat
Rec
A Discov Mol Cell Evol Biol 2003 Jan
PMID:Postnatal maturation of the dog stria vascularis-- an immunohistochemical study. 1249 92
This study investigated the morphological changes of lungs in F344/N rats (9-36 months old). We initially examined general and quantitative morphological changes, and then we used immunohistochemistry to detect distributional changes in collagen subtypes (types I, III, and IV) and smooth muscle cell (SMC) markers (alpha-smooth muscle actin (ASMA), gamma-smooth muscle actin (GSMA), desmin, and
vimentin
) in the lungs. In 24-month-old rats, alveolar ducts and alveolar sacs were enlarged, and alveoli were wider and shallower than in younger animals. In old rats (>/=27 months), terminal and respiratory bronchioles and alveolar ducts were dilated and alveoli were more extended than in 24-month-old rats. No age-related distributional changes were observed for collagen types I, III, and IV as revealed by immunohistochemistry, or elastin as revealed by resorsin fuchsin. SMCs in the extra- and intrapulmonary bronchi were immunoreactive for ASMA, GSMA, and desmin, but not for
vimentin
at all ages. In old rats (>/=27 months), SMCs were loosely arranged in comparison with younger animals, and stainability for GSMA and desmin was decreased. In the respiratory bronchioles and alveolar ducts, a few cells immunoreactive for ASMA and
vimentin
were observed in the smooth muscle aggregations of the alveolar orifice in rats younger than 12 months. In older rats (>20 months), cells immunoreactive for ASMA and
vimentin
were increased in septal tips. In conclusion, extension of distal airways and immunohistochemical changes of SMC markers in F344/N rat lungs were evident by approximately 24 months of age, but there was no apparent change in connective tissue morphology.
Anat
Rec
A Discov Mol Cell Evol Biol 2003 Jun
PMID:Morphology of aging lung in F344/N rat: alveolar size, connective tissue, and smooth muscle cell markers. 1274 Sep 48
We have presented a structural model of the chromosome based on its constituent proteins. Development of a method of mass isolation for intact human metaphase chromosomes and proteome analysis by mass spectrometry of the isolated chromosomal proteins enabled us to develop a four-layer structural model of human metaphase chromosomes. The model consists of four layers, each with different chromosomal protein sets, i.e., chromosome coating proteins (CCPs), chromosome peripheral proteins (CPPs), chromosome structural proteins (CSPs), and chromosome fibrous proteins (CFPs). More than 200 identified proteins have been classified and assigned to the four layers with each layer occupying a distinct region of the chromosome. CCPs are localized at the most outer regions of the chromosomes and they attach to the regions tentatively and occasionally. CCPs include mostly mitochondrial and cytoplasmic proteins, e.g., 70 kDa heat shock protein 9B and Hsp60. CPPs are also localized at the peripheral regions of the chromosomes, but as the essential part of the chromosomes. CPPs include nucleolin, lamin A/C, fibrillarin, etc. CSPs are the primary chromosomal structure proteins, and include topoisomerase IIalpha, condensin subunits, histones, etc. CFPs have a fibrous nature, e.g., beta-actin,
vimentin
, myosin II, tublin, etc. A data set of these proteins, which we developed, contains essential chromosome proteins with classified information based on this four-layer model and presents useful leads for further studies on chromosomal structure and function.
Chem
Rec
2007
PMID:Chromosome protein framework from proteome analysis of isolated human metaphase chromosomes. 1766 45
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