Other

Haemopep Pharma Gmbh

Biovision, Ag

Peter Schulz-Knappe

Wolf-Georg Forssmann

Markus Meyer

Christian Stief

Torsten Strohmeyer

Akmal Taher

Knut Adermann

Hans-Georg Opitz

Franz Herbst

Michael Gagelmann

Michael Schrader

Andreas Pardigol

Hans-Jurgen Magert

A method for detecting the condition of an organism through the measurement of peptides from a sample of said organism containing high- and low-molecular weight peptides, as an indication of the condition of said organism, wherein

Process for determining the status of an organism by peptide measurement

The CC type chemokines belong to a family of polypeptides which have proven to be mediators of immune reactions, and they have recently attracted attention due to their antiviral activity with respect to HIV. The cloning and molecular characterization of a human tandem gene is disclosed which contains the closely linked coding regions for two new CC type chemokines the sequences of which are highly homologous with that of MIP-1&agr;. The transcription of the tandem gene leads to a bicistronic mature transcript which contains the non-overlapping open reading frames for the recently described factor HCC-1 and an as yet unknown CC type chemokine, designated as CC-2. Moreover, alternative splicing of the primary transcript yields at least one additional CC type chemokine, cytokine CC-3. Two functional promoter regions were identified within the tandem gene. The disclosed data provide some basic knowledge about the structure and expression of the new human CC-2/HCC-1 tandem gene and describe a mechanism according to which the coexpression of closely linked genes could be regulated in higher eucaryotes.

Tandem cDNAs encoding chemokines CC-1, CC-2, and CC-3

The invention relates to the use of inhibitors of phosphodiesterase IV for the modulation of the motility and peristalsis of the hollow organs of the urogenital and gastrointestinal tract.

Inhibitors of phosphodiesterase IV for x-ray imaging

Use of inhibitors of phosphodiesterase IV

The invention relates to a peptide from human blood, designated as hPTH-(1-37), the structure of which was elucidated for the purpose of the diagnostic, medical and commercial utilization thereof. The isolation of a fragment hPTH-(38-84) proves the existence of the hPTH-(1-37). A removal of amino-terminal amino acids from the hPTH fragment-(1-37) reduces its biological activity. The hPTH-(1-37) circulating in the blood is identical with the synthetic reference substance hPTH-(1-37), however not with fragments such as hPTH-(1-33), hPTH-(1-34) or hPTH-(1-38). The molecule form hPTH-(1-37) has been proven by mass spectrometry (plasma desorption method). A different biological activity and differences in the three-dimensional peptide structure of the hPTH fragment-(1-37) in comparison to other hPTH fragments furnish evidence of that this fragment is the preferential natural peptide of the parathormone family which should be used for the treatment of diseases of the parathyroid, circulatory system, respiratory system, male genital organ and kidneys.

HPTH-fragment-(1-37), the preparation thereof, medicaments containing

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Hannover, Germany

Peter Schulz-Knappe