Functional expression and signaling properties of cloned human parathyroid hormone receptor in Xenopus oocytes. Evidence for a novel signaling pathway.

Expression of human parathyroid hormone receptor (hPTHR) was obtained in Xenopus oocytes. Receptor function was detected by hormone stimulation of endogenous Ca2+-activated Cl- current. This current was blocked by injected, but not by extracellular, EGTA, confirming that the hPTHR activates cytosolic Ca2+ signaling pathways.

Nucleic acid sequences coding for internal antisense peptides: are there implications for protein folding and evolution?

We have asked whether coding segments of nucleic acids generate amino acid sequences which have an antisense relationship to other amino acid sequences in the same chain (i.e. 'Internal Antisense'), and if so, could the internal antisense content be related to the structure of the encoded protein? Computer searches were conducted with the coding sequences for 132 proteins.

Problems and approaches in covalent attachment of peptides and proteins to inorganic surfaces for biosensor applications.

Some of the fundamental problems in covalent attachment of peptides and proteins to putative biosensor surfaces are reviewed and specific approaches to these problems discussed. In addition, selected aspects of our recent work utilizing self-assembled monolayer (SAM) systems designed to react selectively with the thiol side chain of Cys in proteins are presented. Uniform attachment of a 21-amino acid peptide antigen through a single Cys residue with retention of biological function (antibody binding) has been attained.

Characterization of the interaction of parathyroid hormone with the mitochondrial ATPase.

Parathyroid hormone (PTH) has been shown to bind specifically to the beta subunit of the mitochondrial ATPase on nitrocellulose blots. We have now examined this interaction further, using intact mitochondria, submitochondrial particles, and the purified F1 ATPase. With intact mitochondria, 1 microM concentrations of PTH and its biologically active 1-34 fragment activate the ATPase about 3-fold.

Is genetic code redundancy related to retention of structural information in both DNA strands?

We have noted that the sense-antisense relationships inherent in the genetic code divide the amino acids into three separate groups. The nature of the amino acids in each group may allow the polypeptides coded by the antisense strand to retain the secondary structure patterns of the translated strand. Also, this relationship requires all but eight of the codons in the eukaryotic code and all but four in the mitochondrial code.