Immunohistochemical localization of laminin and type IV collagen in human cutaneous sensory nerve formations

Vega, J. A.; Esteban, I.; Naves, F.J.; Soto, Miguel; Malinovský, L

doi:10.1007/bf00215295

Cited by 25 publications

(26 citation statements)

References 38 publications

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“…At present, little information is available on the localization of these substances in SNF (Ide, 1986;Maeda et al, 1991;Vega et al, 1995). Conversely, the occurrence of laminin and type IV collagen in relation to basement membranes of Schwann, endoneurial and perineurial cells is well documented (de Vellis, 1993; Hslao et al, 1993;Lorimier et al, 1992;Vitellaro-Zuccarello et al, 1992).…”

Section: Type I and Ii If Proteins: Cytokemtina (Ck)mentioning

confidence: 91%

Immunohistochemistry of human cutaneous Meissner and Pacinian corpuscles

Vega

Haro

Soto

1996

Microsc. Res. Tech.

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Section: Type I and Ii If Proteins: Cytokemtina (Ck)mentioning

confidence: 91%

Immunohistochemistry of human cutaneous Meissner and Pacinian corpuscles

Vega

Haro

Soto

1996

Microsc. Res. Tech.

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“…The endoneurial-perineurial capsule, more or less developed, is composed of flattened endoneurial-perineurial cells which also posses basement membranes. The fibrillary structure of the interlamellar spaces in Pacinian corpuscles as well as composition of the basal lamina in Meissner and Pacinian corpuscles was studied using electron microscopy or immunohistochemistry for some of their constituents (see for references Vega et al, 1995a). However, only during the last decade a considerable effort was made to clarify the composition and role of the interlamellar (intercellular) spaces of sensory corpuscles.…”

Section: The Extracellular Matrix and Thementioning

confidence: 99%

The Meissner and Pacinian sensory corpuscles revisited new data from the last decade

Vega

García‐Suárez

Montano

et al. 2008

Microscopy Res & Technique

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This article reviews the biochemical, physiological, and experimental data cumulated during the last decade on the Meissner and Pacinian corpuscles. It includes information about (i) the localization of molecules recently detected in sensory corpuscles; (ii) the unsolved problem of the accessory fibers in sensory corpuscles and the occurrence of myelin within them; (iii) the development of sensory corpuscles, especially their neuronal and growth factor dependency; (iv) the composition and functional significance of the extracellular matrix as an essential part of the mechanisms involved in the genesis of the stimuli generated in sensory corpuscles; (v) the molecular basis of mechanotransduction; (vi) a miscellaneous section containing sparse new data on the protein composition of sensory corpuscles, as well as in the proteins involved in live-death cell decisions; (vii) the changes in sensory corpuscles as a consequence of aging, the central, or peripheral nervous system injury; and finally, (viii) the special interest of Meissner corpuscles and Pacinian corpuscles for pathologists for the diagnosis of some peripheral neuropathies and neurodegenerative diseases.

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“…[19] The authors colocalized S-100 protein and epithelial membrane antigen in parallel with markers such as neurofilament antibody. [19] In the dermal nerve trunks, immunostaining for laminin and type IV collagen was found to colocalize in the perineurium and the Schwann cells, with stronger immunoreactivity at the external surface of the cells. In the Meissner corpuscles, immunoreactivity for laminin and type IV collagen was primarily observed under the cell surface of lamellar cells, while the cytoplasms were weakly immunolabeled or unlabeled.…”

Section: Type IV Collagen and The Skinmentioning

confidence: 99%

Collagen IV in normal skin and in pathological processes

2012

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Context:Type IV collagen is a type of collagen found primarily in the skin within the basement membrane zone. The type IV collagen C4 domain at the C-terminus is not removed in post-translational processing, and the fibers are thus link head-to-head, rather than in a parallel fashion. Also, type IV collagen lacks a glycine in every third amino-acid residue necessary for the tight collagen helix. Thus, the overall collagen-IV conformation is structurally more pliable and kinked, relative to other collagen subtypes. These structural features allow collagen IV to form sheets, which is the primary structural form found in the cutaneous basal lamina. There are six human genes associated with collagen IV, specifically COL4A1, COL4A2, COL4A3, COL4A4, COL4A5 and COL4A6. The aim of this review is to highlight the significance of this protein in normal skin, and in selected diseases.Results:The alpha 3 protein constituent of type IV collagen is thought to be the antigen implicated in Goodpasture's syndrome, wherein the immune system attacks the basement membranes of the renal glomeruli and pulmonary alveoli. In addition, mutations to the genes coding for type IV collagen lead to the Alport syndrome. Furthermore, autoantibodies directed against denatured human type IV collagen have been described in rheumatoid arthritis, scleroderma, and SLE. Structural studies of collagen IV have been utilized to differentiate between subepidermal blistering diseases, including bullous pemphigoid, acquired epidermolysis bullosa, anti-epiligrin cicatricial pemphigoid, and bullous lupus erythematosus. Collagen IV is also of importance in wound healing and in embryogenesis.Conclusions:Pathological studies have demonstrated that minor structural differences in collagen IV can lead to distinct, clinically different diseases.

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Immunohistochemical localization of laminin and type IV collagen in human cutaneous sensory nerve formations

Cited by 25 publications

References 38 publications

Immunohistochemistry of human cutaneous Meissner and Pacinian corpuscles

Immunohistochemistry of human cutaneous Meissner and Pacinian corpuscles

The Meissner and Pacinian sensory corpuscles revisited new data from the last decade

Collagen IV in normal skin and in pathological processes

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