scholarly journals Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments.

1991 ◽  
Vol 114 (3) ◽  
pp. 567-576 ◽  
Author(s):  
P Rousselle ◽  
G P Lunstrum ◽  
D R Keene ◽  
R E Burgeson
Keyword(s):  
Basement Membrane ◽  
Disulfide Bonds ◽  
Human Keratinocytes ◽  
Abundant Species ◽  
Lamina Densa ◽  
Basal Surface ◽  
Type Vii Collagen ◽  
Tissue Region ◽  
Long Rod ◽  
Membrane Adhesion

Basal keratinocytes attach to the underlying dermal stroma through an ultrastructurally unique and complex basement membrane zone. Electron-dense plaques along the basal surface plasma membrane, termed hemidesmosomes, appear to attach directly to the lamina densa of the basement membrane through fine strands, called anchoring filaments. The lamina densa is secured to the stroma through a complex of type VII collagen containing anchoring fibrils and anchoring plaques. We have identified what we believe is a novel antigen unique to this tissue region. The mAbs to this antigen localize to the anchoring filaments, just below the basal-dense plate of the hemidesmosomes. In cell culture, the antigen is deposited upon the culture substate by growing and migrating human keratinocytes. Addition of mAb to the cultures causes the cells to round and detach, but does not impair them metabolically. Skin fragments incubated with antibody extensively de-epithelialize. These findings strongly suggest that this antigen is intimately involved in attachment of keratinocytes to the basement membrane. This antigen was isolated from keratinocyte cultures by immunoaffinity chromatography. Two molecules are observed. The most intact species contains three nonidentical chains, 165, 155, and 140 kD linked by interchain disulfide bonds. The second and more abundant species contains the 165- and 140-kD chains, but the 155-kD chain has been proteolytically cleaved to 105 kD. Likewise, two rotary-shadowed images are observed. The larger of the two, presumably corresponding to the most intact form, appears as an asymmetric 107-nm-long rod, with a single globule at one end and two smaller globules at the other. The more abundant species, presumably the proteolytically cleaved form, lacks the distal small globule. We propose the name "kalinin" for this new molecule.

Kalinin: A new epithelial basement membrane adhesion molecule

1991 ◽  
Vol 49 ◽  
pp. 178-179
Author(s):  
Douglas R. Keene ◽  
Gregory P. Lunstrum ◽  
Patricia Rousselle ◽  
Robert E. Burgeson
Keyword(s):  
Basement Membrane ◽  
Culture Media ◽  
Polyacrylamide Gel Electrophoresis ◽  
Human Keratinocytes ◽  
Positive Staining ◽  
Human Amnion ◽  
Epithelial Basement Membrane ◽  
Type Vii Collagen ◽  
Keratinocyte Cell ◽  
Epithelial Basement

A mouse monoclonal antibody produced from collagenase digests of human amnion was used by LM and TEM to study the distribution and ultrastructural features of an antigen present in epithelial tissues and in cultured human keratinocytes, and by immunoaffinity chromatography to partially purify the antigen from keratinocyte cell culture media.By immunofluorescence microscopy, the antigen displays a tissue distribution similar to type VII collagen; positive staining of the epithelial basement membrane is seen in skin, oral mucosa, trachea, esophagus, cornea, amnion and lung. Images from rotary shadowed preparations isolated by affinity chromatography demonstrate a population of rod-like molecules 107 nm in length, having pronounced globular domains at each end. Polyacrylamide gel electrophoresis suggests that the size of this molecule is approximately 440kDa, and that it is composed of three nonidentical chains disulfide bonded together.

Structure, compositon and function of the dermal-epidermal junction: Relevance in cutaneous disease and diagnosis

1989 ◽  
Vol 47 ◽  
pp. 868-869
Author(s):  
K. A. Holbrook
Keyword(s):  
Basement Membrane ◽  
Epidermolysis Bullosa ◽  
Normal Skin ◽  
Lamina Densa ◽  
Inherited Disorders ◽  
Ultrastructural Studies ◽  
Type Iv ◽  
Type Vii Collagen ◽  
Attachment Structures ◽  
Matrix Components

The dermal-epidermal junction (DEJ), or basement membrane rone, is the boundary between the epithelial and mesenchymal compartments of the skin; epidermal and fibroblastic cells in these two regions collaborate to synthesire its components. Ultrastructural studies (TEM and SEM) have defined a series of planes or layers (basal epidermal, lamina lucida, lamina densa, sublamina densa) and the morphology and density of attachment structures (hemidesmosomes, anchoring filaments, anchoring fibrils and anchoring plaques) in this region of normal skin. Change in structure of the DEJ provides information about the history of the tissue; reduplication of the lamina densa, for example, indicates a site of cell detachment or migration, or remodelling that accompanies repair of focal damage. In normal skin the structure of the DEJ is stable; in pathologic conditions it can be compromised by the congenital absence of certain structures or antigens (e.g., in the inherited disorders, epidermolysis bullosa [EB]) or by enzymatic degradation (e.g., in tumor invasion). Dissolution of the DEJ can also occur normally during the formation of epidermal appendages (e.g., hair follicles) and as melanocytes and Langerhans cells migrate into the epidermis during development.Biochemical and immunohisto/cytochemical studies have identified more than 20 molecules at the DEJ. These include well known matrix molecules (e.g., types IV and V collagen, laminin and fibronectin) and skin-specific antigens. The latter have been identified by autoantibodies or specific polyclonal or monoclonal antibodies raised against the skin, cultured cells and other epithelia. Some of the molecules of the DEJ are are present in basement membrane zones of many epithelia and thus are considered ubiquitous components (type IV, V, laminin, fibronectin, nidogen, entactin, HSPG, LDA-1, CSP [3B3]). All of them (that have been investigated in developing skin) appear ontogenetically as early as human embryonic tissue can be obtained and their expression is typically normal in patients with EB. The known properties of many of these molecules (particularly the matrix components) suggest functions they might impart to the DEJ: support of an epithelium (type IV collagen), regulation of permeability (heparan sulfate proteoglycan) or facilitation of cell attachment (fibronectin) and movement (laminin). Another group of matrix components and antigens of the DEJ includes molecules that are skin-specific or characteristic of stratified squamous epithelia (type VII collagen=LH 7:2 antigen, bullous pemphigoid antigen, AA3, GB3, KF-1,19-DEJ-1, epidermolysis bullosa acquisita antigen [EBA], AF-1 and AF-2, cicatricial pemphigoid antigen [CPA]) . These molecules are expressed in the DEJ later in development than the first group of molecules, in conjunction with the morphologic appearance of the structure they represent. Their appearance is also coordinated with specific developmental events (e.g., epidermal stratification) and the expression of molecules of differentiation in the epidermis and dermis. One or more of them is typically absent or reduced in expression in the skin of patients with heritable disorders affecting this region. There is no apparent correlation between the location of molecules in the DEJ and the stability of their expression.

scholarly journals The Alteration of the Epidermal Basement Membrane Complex of Human Nevus Tissue and Keratinocyte Attachment after High Hydrostatic Pressurization

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Naoki Morimoto ◽  
Chizuru Jinno ◽  
Atsushi Mahara ◽  
Michiharu Sakamoto ◽  
Natsuko Kakudo ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Immunohistochemical Staining ◽  
Human Keratinocytes ◽  
Membrane Complex ◽  
Type Vii Collagen ◽  
Transmission Electron ◽  
Skin Reconstruction ◽  
The Difference ◽  
Laminin 332 ◽  
Epidermal Basement Membrane

We previously reported that human nevus tissue was inactivated after high hydrostatic pressure (HHP) higher than 200 MPa and that human cultured epidermis (hCE) engrafted on the pressurized nevus at 200 MPa but not at 1000 MPa. In this study, we explore the changes to the epidermal basement membrane in detail and elucidate the cause of the difference in hCE engraftment. Nevus specimens of 8 mm in diameter were divided into five groups (control and 100, 200, 500, and 1000 MPa). Immediately after HHP, immunohistochemical staining was performed to detect the presence of laminin-332 and type VII collagen, and the specimens were observed by transmission electron microscopy (TEM). hCE was placed on the pressurized nevus specimens in the 200, 500, and 1000 MPa groups and implanted into the subcutis of nude mice; the specimens were harvested at 14 days after implantation. Then, human keratinocytes were seeded on the pressurized nevus and the attachment was evaluated. The immunohistochemical staining results revealed that the control and 100 MPa, 200 MPa, and 500 MPa groups were positive for type VII collagen and laminin-332 immediately after HHP. TEM showed that, in all of the groups, the lamina densa existed; however, anchoring fibrils were not clearly observed in the 500 or 1000 MPa groups. Although the hCE took in the 200 and 500 MPa groups, keratinocyte attachment was only confirmed in the 200 MPa group. This result indicates that HHP at 200 MPa is preferable for inactivating nevus tissue to allow its reuse for skin reconstruction in the clinical setting.

Immunohistochemical localization of basement membrane type VII collagen and laminin in neoplasms of the head and neck

1992 ◽  
Vol 21 (5) ◽  
pp. 459-464 ◽  
Author(s):  
R.H.W. WETZELS ◽  
L-A. VAN DER VELDEN ◽  
H.E. SCHAAFSMA ◽  
J.J. MANNI ◽  
I.M. LEIGH ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Head And Neck ◽  
Immunohistochemical Localization ◽  
Type Vii Collagen ◽  
Membrane Type

scholarly journals Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen

2009 ◽  
Vol 122 (11) ◽  
pp. 1788-1799 ◽  
Author(s):  
V. L. Martins ◽  
J. J. Vyas ◽  
M. Chen ◽  
K. Purdie ◽  
C. A. Mein ◽  
...  
Keyword(s):  
Squamous Cell Carcinoma ◽  
Basement Membrane ◽  
Cell Carcinoma ◽  
Squamous Cell ◽  
Cutaneous Squamous Cell Carcinoma ◽  
Type Vii Collagen ◽  
Membrane Type

scholarly journals Structural features of alveolar wall basement membrane in the adult rat lung.

1981 ◽  
Vol 91 (2) ◽  
pp. 427-437 ◽  
Author(s):  
C A Vaccaro ◽  
J S Brody
Keyword(s):  
Basement Membrane ◽  
Ruthenium Red ◽  
Basement Membranes ◽  
Alveolar Wall ◽  
Type I ◽  
Type Ii ◽  
Rat Lung ◽  
Anionic Sites ◽  
Lamina Densa ◽  
Adult Rat

The ultrastructural characteristics of alveolar (ABM) and capillary (CBM) basement membranes in the adult rat lung have been defined using tannic acid fixation, ruthenium red staining, or incubation in guanidine HCl. ABM is dense and amorphous, has 3- to 5-nm filaments in the lamina rara externa (facing the alveolus) that run between the lamina densa and the basal cell surface of the epithelium, has an orderly array of ruthenium red-positive anionic sites that appear predominantly (79%) on the lamina rara externa, and has discontinuities beneath alveolar type II cells but not type I cells that allow penetration of type II cytoplasmic processes into the interstitium of the alveolar wall. The CBM is fibrillar and less compact than ABM, has no lamina rara filaments, and has one fifth the number of ruthenium red-positive anionic sites of ABM that appear predominantly (64%) overlying the lamina densa. Incubation of lung tissue with Flavobacterium heparinum enzyme or with chondroitinase has shown that ABM anionic sites represent heparan sulfate proteoglycans, whereas CBM anionic sites contain this and other sulfated proteoglycans. The CBM fuses in a local fashion with ABM, compartmentalizing the alveolar wall into a thick and thin side and establishing a thin, single, basement-membrane gas-exchange surface between alveolar air, and capillary blood. The potential implications of ABM and CBM ultrastructure for permeability, cell differentiation, and repair and morphogenesis of the lung are discussed.

Integrin and basement membrane normalization in mouse grafts of human keratinocytes – Implications for epidermal homeostasis

1997 ◽  
Vol 61 (3) ◽  
pp. 195-209 ◽  
Author(s):  
Dirk Breitkreutz ◽  
Hans-Jürgen Stark ◽  
Heinrich Steinbauer ◽  
Norbert E. Fusenig ◽  
Nicolae Mirancea ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Human Keratinocytes ◽  
Epidermal Homeostasis

scholarly journals Localization and quantitation of anionic charge sites in fetal and neonatal alveolar basement membranes.

1985 ◽  
Vol 33 (6) ◽  
pp. 611-614 ◽  
Author(s):  
T B Ferrara ◽  
S P Sisson ◽  
R L Vernier
Keyword(s):  
Basement Membrane ◽  
Microscopic Analysis ◽  
Basement Membranes ◽  
Lamina Densa ◽  
Human Lung Tissue ◽  
Charge Site ◽  
Electron Microscopic ◽  
Anionic Charge ◽  
Site Localization ◽  
Standard Techniques

A method utilizing biopsy sized samples of lung for anionic charge site localization in alveolar and capillary basement membranes in human tissue is discussed. Tissue fixed in either paraformaldehyde-lysine-periodate or 1% paraformaldehyde with 0.05% glutaraldehyde, cut into 30 mu sections, and incubated with the cationic probe, polyethyleneimine, was processed for electron microscopic analysis using standard techniques. Anionic charge sites were identified and regularly distributed in increments of approximately 40-50 nm in the lamina rara externa of the alveolar basement membrane, with lesser amounts found in the lamina rara interna and lamina densa. Anionic charge sites were also demonstrated in the interstitial portion of the capillary basement membrane and on cell surfaces. These methods can be used to more broadly define the localization of anionic charge sites in human lung tissue in both normal and pathologic states.

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