The genes for the inter-α-inhibitor family share a homologous organization in human and mouse

Inter-α-inhibitor ( IαI ) and related molecules in human are comprised of three evolutionarily related, heavy (H) chains and one light (L) chain, also termed bikunin. The latter originates from a precursor molecule that is cleaved to yield the bikunin and another protein designated α-1-microglobulin (A1m). The four H and L chains are encoded by four distinct genes designated H1, H2, H3 , and L . The L and H2 genes are localized onto human chromosomes (chr) 9 and 10, respectively, whereas the H1 and H3 genes are tandemly arranged on chr 3.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/46989/1/335_2004_Article_BF00355432.pd

HER-2/neu receptor in prostate cancer development and progression to androgen independence.

Development of prostate cancer and progression to androgen-independent disease is correlated with increased expression of growth factors and receptors capable of establishing autocrine and/or paracrine growth-stimulatory loops. A thorough review was made of the current literature and recent abstract presentations at scientific meetings focusing on the role of the HER-2/neu (c-erbB2) receptor in prostate cancer and the potential clinical usefulness of its specific inhibitors. In the past 10 years, conflicting results on HER-2/neu expression in prostate cancer have been reported. More recently, four studies have shown experimental evidence of HER-2/neu in the development of prostate cancer and, more specifically, in the progression to a hormone-refractory clinical behavior. Furthermore, it has been proposed that HER-2 family and androgen receptors function synergistically in the absence of androgen, which suggests a cross-talk between the HER-2/neu and androgen receptor pathways. Finally, clinical trials are in progress in prostate cancer patients to test novel agents that selectively interfere with HER-2/neu activity

Pancreatic secretory trypsin inhibitor in gastrointestinal mucosa and gastric juice.

We studied the distribution of pancreatic secretory trypsin inhibitor (PSTI) in the epithelia of the gastrointestinal tract and determined whether PSTI is secreted into gastric juice. PSTI was measured by a specific radioimmunoassay in biopsy specimens taken from the upper (n = 8) and lower (n = 7) gastrointestinal tract of patients with normal endoscopies. PSTI was present in the stomach, small intestine, and colon. Concentrations (micrograms/g protein) were highest in the stomach, and significantly higher in the antrum (1240, 670-1700, median and range) than in the gastric body (370, 350-570) (p less than 0.01). Concentrations were similar in the duodenum (180, 80-210) and colon (160, 130-360). PSTI determined by immunohistochemistry was present in mucus secreting gastric foveolar cells, duodenal Paneth cells, and colonic non mucus cells. PSTI was present in gastric juice. The median (range) concentration of PSTI in basal gastric juice from 13 patients with duodenal ulcers was 9 (3-21) micrograms/l and did not change during stimulation with pentagastrin. The rate of secretion, however, did increase significantly (p less than 0.05) from 1430 (180-2810) ng/h to 4500 (1250-12,770) ng/h during pentagastrin stimulation. PSTI was labile in acid pepsin but stable in the neutral conditions present in the mucus layer. The presence of pancreatic secretory trypsin inhibitor throughout the gut and its secretion into the lumen suggests a hitherto unrecognised mechanism protecting gastrointestinal epithelia against luminal proteases