Importance of nidogen binding to laminin gamma1 for branching epithelial morphogenesis of the submandibular gland

Development ◽  
1997 ◽  
Vol 124 (3) ◽  
pp. 683-691 ◽  
Author(s):  
Y. Kadoya ◽  
K. Salmivirta ◽  
J.F. Talts ◽  
K. Kadoya ◽  
U. Mayer ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Submandibular Gland ◽  
Driving Forces ◽  
Basement Membranes ◽  
Epithelial Morphogenesis ◽  
Epidermal Growth ◽  
Membrane Components ◽  
Blocking Antibodies

Epithelial-mesenchymal interactions are major driving forces for the development of most solid organs. The importance of these interactions was first shown for the embryonic submandibular gland more than 40 years ago. We here present evidence that interactions between two basement membrane components, nidogen (entactin) and laminin gamma1 chain, could be important for epithelial-mesenchymal interactions in this gland. Nidogen mRNA was detected by in situ hybridization in the mesenchyme, and yet the protein was detected in epithelial and endothelial basement membranes. The role of nidogen-laminin interactions for epithelial morphogenesis was studied by applying antibodies to submandibular gland organ cultures. Antibodies reacting strongly with the nidogen-binding site of laminin gamma1 chain drastically perturbed branching epithelial morphogenesis. Electron microscopy of the epithelial-mesenchymal interface showed that blocking antibodies disrupted the formation of the basement membrane. Epidermal growth factor was shown to increase the expression of nidogen in mesenchyme, and could counteract the effect of the blocking antibodies. We suggest that nidogen could be an important mesenchymal factor for submandibular gland development.

Role of mesenchymal nidogen for epithelial morphogenesis in vitro

Development ◽  
1994 ◽  
Vol 120 (7) ◽  
pp. 2003-2014 ◽  
Author(s):  
P. Ekblom ◽  
M. Ekblom ◽  
L. Fecker ◽  
G. Klein ◽  
H.Y. Zhang ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Northern Blotting ◽  
Epithelial Morphogenesis ◽  
Extracellular Matrix Protein ◽  
Epithelial Development ◽  
Morphogenesis In Vitro ◽  
Development In Vitro ◽  
Membrane Components

Recent biochemical studies suggested that the extracellular matrix protein nidogen is a binding molecule linking together basement membrane components. We studied its expression and role during development. By immunofluorescence and northern blotting, nidogen was found early during epithelial cell development of kidney and lung. Yet, in situ hybridization revealed that nidogen was not produced by epithelium but by the adjacent mesenchyme in both organs. Binding of mesenchymal nidogen to epithelial laminin may thus be a key event during epithelial development. This is supported by antibody perturbation experiments. Antibodies against the nidogen binding site on laminin B2 chain perturbed epithelial development in vitro in embryonic kidney and lung. Mesenchymal nidogen could be important for early stages of epithelial morphogenesis.

Effect of pregestational sialoadenectomy of nursing mothers on eyelid opening of pups

1985 ◽  
Vol 249 (3) ◽  
pp. R285-R289
Author(s):  
S. Okamoto ◽  
T. Oka
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Submandibular Gland ◽  
Mammary Glands ◽  
Submandibular Glands ◽  
Nursing Mothers ◽  
Pregnant Mice ◽  
Epidermal Growth

The eyelid opening of pups born to and nursed by normal mice occurred by the 15th day of birth, whereas pregestational sialoadenectomy (removal of submandibular glands) of nursing mice delayed eyelid opening of their pups by as much as 5 days. Parotidectomy, however, had no effect on eyelid opening. Cross-foster nursing experiments indicated that the cause for delayed eyelid opening of pups was to be found in sialoadenectomized mothers, not their pups. Sialoadenectomized mothers had underdeveloped mammary glands that produced approximately 50% less milk than controls, and the amount of epidermal growth factor in their milk was similarly reduced. When epidermal growth factor, a polypeptide produced by the submandibular gland, was injected daily at a dose of 5 micrograms into sialoadenectomized pregnant mice, the eyelid opening of the pups nursed by their mothers occurred normally. These results are discussed with regard to the possible role of the submandibular gland and epidermal growth factor in neonatal eyelid opening.

In situ localization of mRNA for epidermal growth factor in the submandibular gland of the mouse.

1985 ◽  
Vol 33 (12) ◽  
pp. 1235-1240 ◽  
Author(s):  
E W Gresik ◽  
R M Gubits ◽  
T Barka
Keyword(s):  
In Situ Hybridization ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Submandibular Gland ◽  
Cdna Probe ◽  
Coding Region ◽  
Specific Hybridization ◽  
Epidermal Growth ◽  
Convoluted Tubules

Epidermal growth factor (EGF) is a polypeptide originally isolated from the mouse submandibular gland, where it is localized immunocytochemically in cells of the granular convoluted tubules (GCT). cDNAs encoding the precursor of mouse submandibular EGF have been cloned (Scott et al. Science 221:236, 1983; Gray et al. Nature 303:722, 1983). A fragment of one of these clones, pmegf10, containing the EGF coding region, was tritium-labeled by nick-translation and used as a probe for in situ hybridization to EGF mRNA. A specific hybridization signal for EGF mRNA was seen only in mature or developing GCT cells. The intensity of the signal was stronger in glands of intact males than in females or in castrated males. In glands of castrates treated with testosterone, or of intact females treated with triiodothyronine (T3), the signal was comparable to that in intact males. In glands of males treated with T3 the intensity of the signal was stronger than in untreated males. A weak to moderate signal was seen in developing GCT cells of 20-day-old males but not females. Hybridization for 3 days gave a stronger signal than that for 1 day. No signal was seen in either sex at 10 days of age, or in control preparations exposed to labeled DNA of pBR322. The presence of EGF mRNA exclusively in GCT cells provides strong evidence that these cells are the only site of synthesis of EGF in the submandibular gland. In situ hybridization with this cDNA probe will provide a sensitive method to determine possible cellular sites of EGF production outside of the submandibular gland.

scholarly journals Intracellular accumulation of basement membrane components during morphogenesis of rat submandibular gland.

1989 ◽  
Vol 37 (9) ◽  
pp. 1387-1392 ◽  
Author(s):  
Y Kadoya ◽  
S Yamashina
Keyword(s):  
Basement Membrane ◽  
Submandibular Gland ◽  
Cell Cluster ◽  
Type Iv ◽  
Short Period ◽  
Epithelial Structure ◽  
Intracellular Vesicles ◽  
Membrane Components ◽  
Rat Submandibular Gland ◽  
Terminal Cluster

The distribution of two basement membrane (BM) components, laminin (LN) and type IV collagen (COLL IV), during acino-tubular morphogenesis of rat submandibular gland was examined immunohistochemically to determine the role of BM in the development of acino-tubular structures. On day 14 of gestation, LN could be found only in the BM separating an undifferentiated cell cluster of gland epithelium from surrounding mesenchyme. However, during a short period through days 15 to 17, LN was detected not only in the BM but also in intracellular vesicles of the cells of the terminal cluster. Immunoelectron microscopy showed the intracellular immunoreactive sites to be rough endoplasmic reticulum, indicating that active LN synthesis occurs in the cells of the terminal cluster. Intracellular immunostaining of LN disappeared completely on day 19 with the development of simple epithelium from the cell cluster, even though BM remained reactive. COLL IV also was accumulated in the intracellular vesicles of terminal cluster cells on day 16 of gestation but not on day 19. These results indicate that synthesis of certain BM components is transiently stimulated in gland epithelium before the formation of simple epithelial structure, and that these components are significantly involved in morphogenesis of the submandibular gland.

Extracellular matrix biology in the lung

1996 ◽  
Vol 270 (1) ◽  
pp. L3-L27 ◽  
Author(s):  
S. E. Dunsmore ◽  
D. E. Rannels
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Current Knowledge ◽  
Biological Effects ◽  
Alveolar Epithelium ◽  
Basement Membranes ◽  
Model Systems ◽  
Capillary Endothelium ◽  
Future Research ◽  
Membrane Components

The lung and other organs are comprised of both cellular and extracellular compartments. Interaction of these components modulates physiological function at the organ, cellular, and subcellular levels. Extracellular components in the gas-exchange region of the lung include both noncellular interstitium and basement membranes. Connective tissue elements of the interstitium in part determine ventilatory function by contributions to tissue compliance and to resistance of the diffusion barrier. The basement membrane underlies cells of both the alveolar epithelium and the capillary endothelium; basement membrane components exert biological effects on adjacent cells through receptor-mediated interactions. This review emphasizes current knowledge concerning the composition and biological activity of extracellular matrix in the alveolar region of the lung. Matrix synthesis and turnover are also considered. Directions for future research are suggested in the context of current knowledge of the lung and other model systems.

scholarly journals Basement membrane proteoglycans in glomerular morphogenesis: chondroitin sulfate proteoglycan is temporally and spatially restricted during development.

1993 ◽  
Vol 41 (3) ◽  
pp. 401-414 ◽  
Author(s):  
K J McCarthy ◽  
K Bynum ◽  
P L St John ◽  
D R Abrahamson ◽  
J R Couchman
Keyword(s):  
Basement Membrane ◽  
Chondroitin Sulfate ◽  
Basement Membranes ◽  
Chondroitin Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Electron Microscopic ◽  
Ureteric Buds ◽  
Membrane Components ◽  
Almost All ◽  
Basement Membrane Components

We previously reported the presence of a basement membrane-specific chondroitin sulfate proteoglycan (BM-CSPG) in basement membranes of almost all adult tissues. However, an exception to this ubiquitous distribution was found in the kidney, where BM-CSPG was absent from the glomerular capillary basement membrane (GBM) but present in other basement membranes of the nephron, including collecting ducts, tubules, Bowman's capsule, and the glomerular mesangium. In light of this unique pattern of distribution and of the complex histoarchitectural reorganization occurring during nephrogenesis, the present study used light and electron microscopic immunohistochemistry to examine the distribution of BM-CSPG and basement membrane heparan sulfate proteoglycan (BM-HSPG) during prenatal and postnatal renal development in the rat. Our results show that the temporal and spatial pattern of expression of BM-CSPG during nephrogenesis is unlike that reported for other basement membrane components such as laminin, fibronectin, and BM-HSPG, all of which can be found in the earliest formed basement membranes of the vesicle-stage nephron. Although BM-CSPG is present in the basement membranes of the invading vasculature and ureteric buds, its first appearance in nephron basement membrane occurs during the late comma stage. In capillary loop-stage glomeruli of prenatal animals, BM-CSPG is present in the presumptive mesangial matrix but undetectable in the GBM. However, as postnatal glomerular maturation progresses BM-CSPG is also found in both the lamina rara interna and lamina densa of the GBM in progressively increasing amounts, being most evident in the GBM of 21-day-old animals. Micrographs of glomeruli from 42-day-old animals show that BM-CSPG gradually disappears from the GBM and, by 56 days after birth, appears to be completely absent from the GBM, its pattern of distribution resembling that of the adult animal. Our results show that BM-CSPG is not required for the initial assembly of basement membranes but may in fact serve to stabilize basement membrane structure after histoarchitectural reorganization is completed.

Epithelial-mesenchymal interactions in the production of basement membrane components in the gut

Development ◽  
1988 ◽  
Vol 102 (2) ◽  
pp. 339-347 ◽  
Author(s):  
P. Simon-Assmann ◽  
F. Bouziges ◽  
C. Arnold ◽  
K. Haffen ◽  
M. Kedinger
Keyword(s):  
Basement Membrane ◽  
Experimental Model ◽  
Type Iv Collagen ◽  
Mesenchymal Cell ◽  
Linear Pattern ◽  
Cellular Origin ◽  
Type Iv ◽  
Species Specific ◽  
Membrane Components

The production and deposition of extracellular matrix proteins and the cellular origin of type-IV collagen have been analysed immunocytochemically in cocultured or transplanted intestinal epithelial-mesenchymal cell associations. In the first experimental model, rat intestinal endodermal cells were cultured on top of confluent monolayers of rat intestinal or skin fibroblastic cells. Under these conditions, interstitial matrix and basement membrane proteins were deposited within the fibroblastic layer over the whole culture period; interactions between the epithelial cells and the fibroblastic cell population, whatever their organ of origin, were required for the production of the basement membrane. In addition, its formation was progressive as assessed by the shift of a spot-like labelling to a continuous linear pattern at the epithelial-mesenchymal interface, and paralleled epithelial cell differentiation. In the second experimental model, chick-rat epithelial-mesenchymal recombinants developed as intracoelomic grafts were used, and the immunocytochemical detection of a basement membrane protein, type-IV collagen, was performed with species-specific antibodies. The major role of the mesenchyme in the deposition of type-IV collagen is supported by the fact that anti-chick but not anti-mammalian antibodies stained this antigen in chick mesenchyme-rat endoderm recombinants. These observations emphasize the role of tissue interactions in the formation of a basement membrane and show that the mesenchymal compartment is the principal endogenous source of type-IV collagen.

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