Laminin chains in rat and human peripheral nerve: Distribution and regulation during development and after axonal injury

Wallquist, Wilhelm; Patarroyo, Manuel Elkín; Thams, Sebastian; Carlstedt, Thomas; Stark, Birgit; Cullheim, Staffan; Hammarberg, Henrik

doi:10.1002/cne.10434

Cited by 73 publications

(65 citation statements)

References 113 publications

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“…This is in contrast to what has been found in dy/dy mice, which lack laminin-2 and display a moderate myelination defect in some parts of the CNS (Chun et al, 2003). In peripheral nerves however, the laminin ␣4 chain is likely present in the basal lamina as the ␣ chain in laminin-8 (Wallquist et al, 2002). Given the fact that a large part of human cases of peripheral neuropathy remains etiologically unknown, and also that a defect in laminin ␣2 production is seen in the human disease MDCMD, it may well be that also laminin ␣4 has a human correlate involving a peripheral neuropathy.…”

Section: Discussioncontrasting

confidence: 81%

“…In a previous study we have shown that the endoneurial basal lamina of peripheral nerves not only contains laminin-2 (␣2␤1␥1) but also laminin-8 (␣4␤1␥1) (Wallquist et al, 2002). Considering the profound effects of laminin-2 deficiency and the importance of basal lamina proteins for cellular interactions, it is of obvious importance to elucidate the function of laminin-8 in the peripheral nerve.…”

Section: Introductionmentioning

confidence: 99%

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Impeded Interaction between Schwann Cells and Axons in the Absence of Laminin α4

Wallquist¹,

Plantman²,

Thams³

et al. 2005

J. Neurosci.

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The Schwann cell basal lamina (BL) is required for normal myelination. Loss or mutations of BL constituents, such as laminin-2 (␣2␤1␥1), lead to severe neuropathic diseases affecting peripheral nerves. The function of the second known laminin present in Schwann cell BL, laminin-8 (␣4␤1␥1), is so far unknown. Here we show that absence of the laminin ␣4 chain, which distinguishes laminin-8 from laminin-2, leads to a disturbance in radial sorting, impaired myelination, and signs of ataxia and proprioceptive disturbances, whereas the axonal regenerative capacity is not influenced. In vitro studies show poor axon growth of spinal motoneurons on laminin-8, whereas it is extensive on laminin-2. Schwann cells, however, extend longer processes on laminin-8 than on laminin-2, and, in contrast to the interaction with laminin-2, solely use the integrin receptor ␣6␤1 in their interaction with laminin-8. Thus, laminin-2 and laminin-8 have different critical functions in peripheral nerves, mediated by different integrin receptors.

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Section: Discussioncontrasting

confidence: 81%

Section: Introductionmentioning

confidence: 99%

Impeded Interaction between Schwann Cells and Axons in the Absence of Laminin α4

Wallquist¹,

Plantman²,

Thams³

et al. 2005

J. Neurosci.

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“…Performance in the behavioral tests was most severely compromised in the DKO, with trembling on the beam, ataxia, and slipping of the hindlimbs, and this was apparently attributable to a more prominent delay in the axonal segregation and a more pronounced lack of C-fibers relative to the Lam␣4 Ϫ/Ϫ mice. Laminin ␣4 is mainly expressed in immature, developing nerves (Patton et al, 1997;Nakagawa et al, 2001;Wallquist et al, 2002), which may account for the partial recovery of the axonal segregation observed in the Lama4 Ϫ/Ϫ mice over 1 year of age. Nonsegregated axons are prominent in both young and old DKO mice, signifying a permanent defect attributable to the absence of the normally constitutively expressed collagen XV.…”

Section: Discussionmentioning

confidence: 99%

Lack of Collagen XV Impairs Peripheral Nerve Maturation and, When Combined with Laminin-411 Deficiency, Leads to Basement Membrane Abnormalities and Sensorimotor Dysfunction

Rasi

Hurskainen²,

Kallio³

et al. 2010

J. Neurosci.

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Although the Schwann cell basement membrane (BM) is required for normal Schwann cell terminal differentiation, the role of BMassociated collagens in peripheral nerve maturation is poorly understood. Collagen XV is a BM zone component strongly expressed in peripheral nerves, and we show that its absence in mice leads to loosely packed axons in C-fibers and polyaxonal myelination. The simultaneous lack of collagen XV and another peripheral nerve component affecting myelination, laminin ␣4, leads to severely impaired radial sorting and myelination, and the maturation of the nerve is permanently compromised, contrasting with the slow repair observed in Lama4 Ϫ/Ϫ single knock-out mice. Moreover, the Col15a1 Ϫ/Ϫ ;Lama4 Ϫ/Ϫ double knock-out (DKO) mice initially lack C-fibers and, even over 1 year of age have only a few, abnormal C-fibers. The Lama4 Ϫ/Ϫ knock-out results in motor and tactile sensory impairment, which is exacerbated by a simultaneous Col15a1 Ϫ/Ϫ knock-out, whereas sensitivity to heat-induced pain is increased in the DKO mice. Lack of collagen XV results in slower sensory nerve conduction, whereas the Lama4 Ϫ/Ϫ and DKO mice exhibit increased sensory nerve action potentials and decreased compound muscle action potentials; x-ray diffraction revealed less mature myelin in the sciatic nerves of the latter than in controls. Ultrastructural analyses revealed changes in the Schwann cell BM in all three mutants, ranging from severe (DKO) to nearly normal (Col15a1 Ϫ/Ϫ ). Collagen XV thus contributes to peripheral nerve maturation and C-fiber formation, and its simultaneous deletion from neural BM zones with laminin ␣4 leads to a DKO phenotype distinct from those of both single knock-outs.

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“…Many nerve ECM molecules such as WARP (5), laminins (22), and nidogens (23) are expressed highly during early development and myelination but are down-regulated at the transcriptional level in adult nerve tissues except in response to injury (22,23). A disorganization of collagen networks in nerve, therefore, may not necessarily undergo repair because it is not severe enough to compromise many normal functions.…”

Section: Discussionmentioning

confidence: 99%

Mice Lacking the Extracellular Matrix Protein WARP Develop Normally but Have Compromised Peripheral Nerve Structure and Function

Allen

Zamurs

Brachvogel

et al. 2009

Journal of Biological Chemistry

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WARP is a recently identified extracellular matrix molecule with restricted expression in permanent cartilages and a distinct subset of basement membranes in peripheral nerves, muscle, and the central nervous system vasculature. WARP interacts with perlecan, and we also demonstrate here that WARP binds type VI collagen, suggesting a function in bridging connective tissue structures. To understand the in vivo function of WARP, we generated a WARPdeficient mouse strain. WARP-null mice were healthy, viable, and fertile with no overt abnormalities. Motor function and behavioral testing demonstrated that WARP-null mice exhibited a significantly delayed response to acute painful stimulus and impaired fine motor coordination, although general motor function was not affected, suggesting compromised peripheral nerve function. Immunostaining of WARP-interacting ligands demonstrated that the collagen VI microfibrillar matrix was severely reduced and mislocalized in peripheral nerves of WARP-null mice. Further ultrastructural analysis revealed reduced fibrillar collagen deposition within the peripheral nerve extracellular matrix and abnormal partial fusing of adjacent Schwann cell basement membranes, suggesting an important function for WARP in stabilizing the association of the collagenous interstitial matrix with the Schwann cell basement membrane. In contrast, other WARP-deficient tissues such as articular cartilage, intervertebral discs, and skeletal muscle showed no detectable abnormalities, and basement membranes formed normally. Our data demonstrate that although WARP is not essential for basement membrane formation or musculoskeletal development, it has critical roles in the structure and function of peripheral nerves. (3), and in the present study we identify type VI collagen as a ligand for WARP. WARP has a restricted distribution in developing cartilage tissues, where it is expressed at sites of joint cavitation and articular cartilage formation rather than cartilage structures that will undergo endochondral ossification (3). In adult tissues, WARP is highly restricted to the chondrocyte pericellular matrix in articular cartilage and fibrocartilages, where it colocalizes with perlecan and collagen VI (3). Several of the major basement membrane components have been found in the chondrocyte pericellular matrix, suggesting that this structure may be the functional equivalent of a basement membrane in cartilage tissues (4). Consistent with this hypothesis, recent data from our laboratory have demonstrated that WARP is a component of the basement membrane in a limited subset of tissues including the apical ectodermal ridge, the endomysium surrounding muscle fibers, the vasculature of the central nervous system, and the endoneurium of peripheral nerves (5). The principal components of basement membranes are type IV collagen, laminins, nidogens, and proteoglycans including perlecan; however, the composition, structure, and biological properties of basement membranes can differ considerably between different tissues (6,...

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Laminin chains in rat and human peripheral nerve: Distribution and regulation during development and after axonal injury

Cited by 73 publications

References 113 publications

Impeded Interaction between Schwann Cells and Axons in the Absence of Laminin α4

Impeded Interaction between Schwann Cells and Axons in the Absence of Laminin α4

Lack of Collagen XV Impairs Peripheral Nerve Maturation and, When Combined with Laminin-411 Deficiency, Leads to Basement Membrane Abnormalities and Sensorimotor Dysfunction

Mice Lacking the Extracellular Matrix Protein WARP Develop Normally but Have Compromised Peripheral Nerve Structure and Function

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