Laminin–a glycoprotein from basement membranes.

Timpl, Rupert; Rohde, Heilwig; Robey, Pamela Gehron; Rennard, Stephen I.; Foidart, Jean‐Michel; Martin, George R.

doi:10.1016/s0021-9258(19)83607-4

Cited by 2,161 publications

(258 citation statements)

References 16 publications

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“…Laminin was first described as a component in the stroma of the EHS tumor (Timpl et al 1979) and the extracellular deposit of murine parietal endoderm PYS cells (Chung et al 1977(Chung et al ,1979. The purified large glycoprotein was named laminin, now referred to as laminin-1, and for several years was the only laminin isoform reported.…”

Section: New Additions To the Laminin Familymentioning

confidence: 99%

Still More Complexity in Mammalian Basement Membranes

Erickson

Couchman

2000

J Histochem Cytochem.

268

193

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At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new α-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.

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Section: New Additions To the Laminin Familymentioning

confidence: 99%

Still More Complexity in Mammalian Basement Membranes

Erickson

Couchman

2000

J Histochem Cytochem.

268

193

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“…More recently, Choi et al studied the influence on osseointegration of an active, laminin-derived peptide (Ln2-P3) in a rabbit tibia model [ 49 ]. Laminin is an ECM protein mainly involved in the mechanism of adhesion and proliferation of basal lamina cells [ 51 ]. Authors equally divided 16 titanium dental implants characterized by SLA surface in two groups, according to the presence or absence of 1 mg/cm 2 Ln2-P3 immobilized on the surface.…”

Section: Biomolecules Used In In Vivo Studiesmentioning

confidence: 99%

Biochemical Modification of Titanium Oral Implants: Evidence from In Vivo Studies

2021

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The discovery of osseointegration of titanium implants revolutionized the dental prosthesis field. Traditionally, implants have a surface that is processed by additive or subtractive techniques, which have positive effects on the osseointegration process by altering the topography. In the last decade, innovative implant surfaces have been developed, on which biologically active molecules have been immobilized with the aim of increasing stimulation at the implant–biological tissue interface, thus favoring the quality of osseointegration. Among these molecules, some are normally present in the human body, and the techniques for the immobilization of these molecules on the implant surface have been called Biochemical Modification of Titanium Surfaces (BMTiS). Different techniques have been described in order to immobilize those biomolecules on titanium implant surfaces. The aim of the present paper is to present evidence, available from in vivo studies, about the effects of biochemical modification of titanium oral implants on osseointegration.

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“…The primary antibody used was a monoclonal laminin antibody (Chemicon). Laminin is a basic component of the basement membrane in the wall of blood vessels 32 and immunostaining for laminin is a reliable method for the detection of blood vessels in dense connective tissue. 14,17 Sections were labeled with the respective secondary antibody, fluorescein thiocyanate conjugated (FITC) goat anti-rabbit IgG (Medac, Hamburg) for 45 minutes.…”

Section: Immunohistochemistrymentioning

confidence: 99%

Blood Supply of the Flexor Hallucis Longus Tendon with Regard to Dancer's Tendinitis: Injection and Immunohistochemical Studies of Cadaver Tendons

et al. 2003

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The flexor hallucis longus is the most common site of lower extremity tendon disorders in ballet dancers. Reduced vascularity is an important factor contributing to tendon degeneration and rupture under strain. A study was conducted on the vascular pattern of the human flexor hallucis longus tendon with injection techniques and immunohistochemically by using antibodies against laminin. Blood supply arose from the posterior tibial and the medial plantar artery. Peritendinous blood vessels penetrated the tendon and anastomosed with a longitudinally oriented intratendinous network. Injection specimens and immunohistochemistry revealed one avascular zone in which the tendon passed behind the talus and a second in which the tendon wrapped around the first metatarsal head. These are the most typical areas for tendon degeneration and rupture.

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Laminin–a glycoprotein from basement membranes.

Cited by 2,161 publications

References 16 publications

Still More Complexity in Mammalian Basement Membranes

Still More Complexity in Mammalian Basement Membranes

Biochemical Modification of Titanium Oral Implants: Evidence from In Vivo Studies

Blood Supply of the Flexor Hallucis Longus Tendon with Regard to Dancer's Tendinitis: Injection and Immunohistochemical Studies of Cadaver Tendons

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