The purpose of this study was to investigate collagen receptors on primary
bovine articular chondrocytes from full-thickness and different layers of b
ovine articular cartilage. Cytometric studies with antibodies showed that a
pproximately 56% of the chondrocytes from the superficial layer and 29% of
the chondrocytes from the deep layer bound anti-annexin V. A similar tenden
cy was found for alpha 5 and beta 1 integrin antibodies. Flow cytometric an
alysis initially detected annexin V on chondrocytes following isolation; th
e level of detection subsequently decreased by 24 hours, whereas that of al
pha 5 and beta 1 integrins increased. Treatment of chondrocytes with collag
enase at 24 hours restored the initially high epitope recognition of annexi
n V, indicating masking of annexin V by newly formed collagen matrix. There
was little effect on detection levels for beta 1 integrin. Contrary to the
specific matrix receptor expression, chondrocytes from superficial and dee
p layers differed little in attachment to immobilized types I and II collag
ens. However, the attachment was more effectively inhibited with anti-annex
in V than with integrin antibodies. Competition studies with preparations o
f soluble collagens revealed a preferential binding of bovine type-II colla
gen compared with bovine type-I collagen. Anti-annexin V antibodies inhibit
ed binding of type-II collagen more effectively than anti-alpha 5 or anti-b
eta 1 integrin antibodies. Evidently, under the in vitro conditions of this
study, annexin V is the quantitatively predominant type-II collagen recept
or on bovine articular chondrocytes. This opens a discussion of the possibl
y dualistic metabolic/mechanical annexin V-integrin receptor elements.