Pharmacological Treatment of Alopecia

In this chapter, we will explore non-surgical treatments of alopecia. Unlike many other areas of medicine, pharmacological treatments for alopecia are relatively new. There are only two treatments which are approved by the Food and Drug Administration (FDA); the rest are drugs developed for other indications which have gained popular off-label use to promote hair growth. The reasons for this are many, including the designation of alopecia by the FDA as a cosmetic disease. This designation has restricted alopecia development programs to compounds with virtually no side effects. Unfortunately, it has also led to off-label use of far more dangerous compounds as alopecia treatments, without the benefit of controlled trials. There is a growing recognition that alopecia, particularly alopecia areata and chemotherapy-induced alopecia, are disorders which significantly alter the quality of life, similar to acne vulgaris and psoriasis, and merit treatment accordingly. There have also been several recent advances in our understanding of the hair cycle, revealing new targets for developing alopecia therapies. As a result, there is a more robust slate of programs for developing new pharmacological treatments for alopecia. In this chapter, we will review current pharmacological treatments for alopecia and selected treatments under development (i.e., those with significant preclinical or clinical data which have appeared in the published literature)

Fusion proteins of collagen-binding domain and parathyroid hormone

Fusion proteins containing active agonist or antagonist fragments of parathyroid hormone (PTH) and parathyroid hormone related peptide (PTHrP) coupled to a collagen-binding domain are presented. The fusion proteins can be used to promote bone growth, to promote hair growth, to prevent cancer metastasis to bone, to promote immune reconstitution with a bone marrow stem cell transplant, to promote mobilization of bone marrow stem cells for collection for autologous stem cell transplant, and to treat renal osteodystrophy. Pharmaceutical agents comprising a collagen-binding polypeptide segment linked to a non-peptidy

Fusion proteins of collagen-binding domain and parathyroid hormone

Fusion proteins containing active agonist or antagonist fragments of parathyroid hormone (PTH) and parathyroid hormone related peptide (PTHrP) coupled to a collagen-binding domain are presented. The fusion proteins can be used to promote bone growth, to promote hair growth, to prevent cancer metastasis to bone, to promote immune reconstitution with a bone marrow stem cell transplant, to promote mobilization of bone marrow stem cells for collection for autologous stem cell transplant, and to treat renal osteodystrophy. Pharmaceutical agents comprising a collagen-binding polypeptide segment linked to a non-peptidyl PTH/PTHrP receptor agonist or antagonist are also presented

Fusion proteins of collagen-binding domain and parathyroid hormone

Fusion proteins containing active agonist or antagonist fragments of parathyroid hormone (PTH) and parathyroid hormone related peptide (PTHrP) coupled to a collagen-binding domain are presented. The fusion proteins can be used to promote bone growth, to promote hair growth, to prevent cancer metastasis to bone, to promote immune reconstitution with a bone marrow stem cell transplant, to promote mobilization of bone marrow stem cells for collection for autologous stem cell transplant, and to treat renal osteodystrophy. Pharmaceutical agents comprising a collagen-binding polypeptide segment linked to a non-peptidyl PTH/PTHrP receptor agonist or antagonist are also presented

Small Molecule Inhibited Parathyroid Hormone Mediated cAMP Response by N–Terminal Peptide Binding

Ligand binding to certain classes of G protein coupled receptors (GPCRs) stimulates the rapid synthesis of cAMP through G protein. Human parathyroid hormone (PTH), a member of class B GPCRs, binds to its receptor via its N–terminal domain, thereby activating the pathway to this secondary messenger inside cells. Presently, GPCRs are the target of many pharmaceuticals however, these drugs target only a small fraction of structurally known GPCRs (about 10%). Coordination complexes are gaining interest due to their wide applications in the medicinal field. In the present studies we explored the potential of a coordination complex of Zn(II) and anthracenyl–terpyridine as a modulator of the parathyroid hormone response. Preferential interactions at the N–terminal domain of the peptide hormone were manifested by suppressed cAMP generation inside the cells. These observations contribute a regulatory component to the current GPCR–cAMP paradigm, where not the receptor itself, but the activating hormone is a target. To our knowledge, this is the first report about a coordination complex modulating GPCR activity at the level of deactivating its agonist. Developing such molecules might help in the control of pathogenic PTH function such as hyperparathyroidism, where control of excess hormonal activity is essentially required