Collagen binding induces changes in its platelet integrin receptor alpha2beta1.

Integrins can signal upon binding of their ligand, presumably because of conformational changes induced by ligand-binding. It has been postulated that ligand binding causes changes in the affinity of the integrin to its ligand. In order to test for ligand-induced change in the affinity of platelet alpha2beta1 to collagen, labelled viable platelets were passaged through a column of fibrillar collagen and stringent lysis conditions were used to remove all low-affinity receptors.

Long-term antibiotic treatment in geriatric diabetic foot infection.

A case report involving a 77-year old diabetic patient with an arterial foot ulcer and subsequent osteomyelitic infection is presented. Due to the patient's ineligibility for surgical intervention, long term antibiotic treatment based upon multiple culture, bone biopsy, radiograms and isotope scanning was initiated. Complete resolution of the osteomyelitis defined by subjective as well as objective criteria was achieved after three months of antibiotic treatment.

Affinity modulation in platelet alpha 2 beta 1 following ligand binding.

In order to test for ligand-induced change in the affinity of platelet alpha 2 beta 1 to collagen we passaged labeled viable platelets through a column of fibrillar collagen and used stringent lysis conditions to remove all low-affinity receptors. A high affinity fraction left on the collagen could be eluted with DTT and 2% SDS. Antibodies raised against it Western-blotted alpha 2 beta 1.