A comparison of serum harvesting methods and type of refractometer for determining total solids to estimate failure of passive transfer in calves.

Monitoring the passive transfer of immunoglobulins from colostrums particularly in noncentrifuged samples can be useful for calf health management programs. The results of total solids refractometry from centrifuge and noncentrifuge harvested sources of serum were highly correlated (R2 = 0.95). Results from a digital and a hand-held refractometer were highly correlated (R2 = 0.96).

Prevalence of Cryptosporidium parvum infection in southwestern Ontario and its association with diarrhea in neonatal dairy calves.

Cryptosporidium parvum infection was detected in 203 (40.6%) of 500 Ontario dairy calves aged 7 to 21 d, on a convenience sample of 51 farms with a history of calf diarrhea. Within-farm prevalence ranged from 0% to 70%, and both shedding and intensity of shedding were significantly associated with diarrhea. This parasite appears to be common in Ontario dairy calves and important as a cause of dairy calf scours in the province.

Integrin alpha2beta1 on rat myeloma cells modulates interaction of alpha4beta1 integrin with vascular cell adhesion molecule-1 but not fibronectin.

It is well established that alpha2beta1 integrin functions as a receptor for collagen and laminin; whereas alpha4beta1 integrin binds fibronectin and vascular cell adhesion molecule-1 (VCAM-1). In the present study, we showed that rat myeloma YB2/0 cells constitutively expressed alpha4beta1 but not alpha2beta1 integrin. Transfection of cDNA of mouse a2 integrin subunit resulted in the expression of heterologous alpha2beta1 integrin on YB2/0 cells (YBmalpha2). The expression of alpha2beta1 conferred YBmalpha2 cells the ability to interact with collagen and laminin. In comparison with mock transfected YB2/0 cells (YBpF), YBmalpha2 cells exhibited increases in the binding and migration on VCAM-1; in contrast, both YBpF and YBmalpha2 were similar in their interactions with fibronectin or fibronectin fragment FN-40 that contains the binding site for alpha4beta1 integrin. The interaction of alpha4beta1 with VCAM-1 was further stimulated upon ligation with alpha2beta1-specific mAb. The use of specific inhibitory mAb demonstrated the role of alpha4beta1 in mediating the observed interactions with fibronectin and VCAM-1. Therefore, results show that expression of alpha2beta1 differentially regulated alpha4alpha1 integrin function by stimulating its interactions with VCAM-1 but not fibronectin. The in vivo significance of alpha2beta1 integrin expression was demonstrated by intravital videomicroscopy showing that ligation of alpha2beta1 enhanced alpha4beta1-mediated extravasation of YBmalpha2 cells in the liver.