Identification and Immunolocalization of Laminin in Cartilage

Dürr, J.; Lammi, Pirkko; Goodman, Simon L.; Aigner, Thomas; Mark, Klaus von der

doi:10.1006/excr.1996.0028

Cited by 67 publications

(57 citation statements)

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“…The results of this study provide evidence for sitespecific variations of the elastic modulus within the PCM. For example, the PCM elastic moduli in this study (56)(57)(58)(59)(60)(61)(62)(63)(64)(65)(66)(67)(68) were approximately twice as stiff as those measured in situ via AFM for porcine cartilage (approx. 30 kPa) in our previous study [38].…”

Section: Discussionmentioning

confidence: 64%

Immunofluorescence-guided atomic force microscopy to measure the micromechanical properties of the pericellular matrix of porcine articular cartilage

Wilusz

DeFrate

Guilak

2012

J. R. Soc. Interface.

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The pericellular matrix (PCM) is a narrow region that is rich in type VI collagen that surrounds each chondrocyte within the extracellular matrix (ECM) of articular cartilage. Previous studies have demonstrated that the chondrocyte micromechanical environment depends on the relative properties of the chondrocyte, its PCM and the ECM. The objective of this study was to measure the influence of type VI collagen on site-specific micromechanical properties of cartilage in situ by combining atomic force microscopy stiffness mapping with immunofluorescence imaging of PCM and ECM regions in cryo-sectioned tissue samples. This method was used to test the hypotheses that PCM biomechanical properties correlate with the presence of type VI collagen and are uniform with depth from the articular surface. Control experiments verified that immunolabelling did not affect the properties of the ECM or PCM. PCM biomechanical properties correlated with the presence of type VI collagen, and matrix regions lacking type VI collagen immediately adjacent to the PCM exhibited higher elastic moduli than regions positive for type VI collagen. PCM elastic moduli were similar in all three zones. Our findings provide further support for type VI collagen in defining the chondrocyte PCM and contributing to its biological and biomechanical properties.

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Section: Discussionmentioning

confidence: 64%

Immunofluorescence-guided atomic force microscopy to measure the micromechanical properties of the pericellular matrix of porcine articular cartilage

Wilusz

DeFrate

Guilak

2012

J. R. Soc. Interface.

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“…Kvist et al (2008) reported that laminin, initially being widespread in newborn cartilage, organized into a pericellular distribution around the chondrocytes in mature cartilage. Similar to the location pattern in the superficial layer of adult articular cartilage, most laminins were detected in the resting zone in epiphyseal cartilage and expression decreased in the proliferating and hypertrophic zones (Dürr et al, 1996;Ustünel et al, 2003a). These findings indicate that laminins are dynamically expressed in a spatiotemporal manner.…”

Section: Y Sun Et Almentioning

confidence: 68%

“…Dürr et al (1996) demonstrated that laminins were mainly located in the PCM of human adult articular cartilage, which was further verified in goat and bovine cartilage Kvist et al, 2008). Ustünel et al (2003b) found a similar pattern of laminin expression in human nasal septal cartilage with higher expression in the periphery of the cartilage, which gradually decreased in deeper zones.…”

Section: Adult Stagementioning

confidence: 82%

“…The expression of laminins varies during different developmental stages of cartilage and cartilage-like tissues ( Fig. 2) (Dürr et al, 1996;Foldager et al, 2016;Lee et al, 1997).…”

Section: Y Sun Et Almentioning

confidence: 99%

“…Developing stage A diverse distribution pattern of laminins was found in different developing stages of cartilage (Dürr et al, 1996;Häusler et al, 2002). Lee et al, (1997) found that laminin chains (α1, α2, β1, β2 and γ1), produced by chicken embryo sternal chondrocytes, exhibited an increased expression in aggregated cells during the maturation stage; LM-111 was detected primarily in the cytoplasm, rather than in the matrix of cartilaginous tissues.…”

Section: Y Sun Et Almentioning

confidence: 99%

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The role of laminins in cartilaginous tissues: from development to regeneration

Sun¹,

Wang²,

Toh³

et al. 2017

eCM

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As a key molecule of extracellular matrix, laminin provides a delicate microenvironment for cell functions. Recent findings suggest that laminins expressed by cartilage-forming cells (chondrocytes, progenitor cells and stem cells) could promote chondrogenesis. However, few papers outline the effect of laminins on providing a favorable matrix microenvironment for cartilage regeneration. In this review, we delineated the expression of laminins in hyaline cartilage, fibrocartilage and cartilage-like tissue (nucleus pulposus) throughout several developmental stages. We also examined the effect of laminins on the biological activities of chondrocytes, including adhesion, migration and survival. Furthermore, we scrutinized the potential influence of various laminin isoforms on cartilage-forming cells' proliferation and chondrogenic differentiation. With this information, we hope to facilitate an understanding of the spatial and temporal interactions between cartilage-forming cells and laminin microenvironment to eventually advance cell-based cartilage engineering and regeneration.

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Laminins: Structure and genetic regulation

Tunggal

Smyth

Paulsson

et al. 2000

Microsc. Res. Tech.

170

128

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The laminins form a large family of modular proteins found in basement membranes, but also elsewhere. They function as structural components and are essential for morphogenesis, but in addition interact with cell surface receptors such as integrins and α‐dystroglycan. By virtue of their receptor interactions, they initiate intracellular signalling events that regulate cellular organization and differentiation. The many interactions of laminins are mediated by binding sites, often contributed by single domains, which may differ between different forms of laminin. In the present article, we describe how the diversity of laminins and the genetic regulation of the expression of different laminin forms lead to the formation of extracellular matrices with variable laminin composition and thereby different biological properties. Microsc. Res. Tech. 51:214–227, 2000. © 2000 Wiley‐Liss, Inc.

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Identification and Immunolocalization of Laminin in Cartilage

Cited by 67 publications

References 0 publications

Immunofluorescence-guided atomic force microscopy to measure the micromechanical properties of the pericellular matrix of porcine articular cartilage

Immunofluorescence-guided atomic force microscopy to measure the micromechanical properties of the pericellular matrix of porcine articular cartilage

The role of laminins in cartilaginous tissues: from development to regeneration

Laminins: Structure and genetic regulation

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