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On World Diabetes Day, Human BioSciences Pledge to Help People Fight from Diabetic Foot Ulcers

DFUs are also characterized by reduced growth factor production and decreased or impaired angiogenic response, macrophage function, collagen accumulation, and epidermal barrier function.

Published: November 14, 2022 11:22 PM IST

By News Desk | Edited by Victor Dasgupta

World Diabetes Day
World Diabetes Day

New Delhi: One of the most common complications of diabetes (DM) is slow-healing wounds, often found on the plantar aspect of the foot, due to the changes in the peripheral circulation, sensation, and structural integrity of the foot common with Type II Diabetes. Diabetic foot wounds (DFU) are notoriously difficult to heal, affected by infection, ischemia, and patient compliance.

“Diabetic Ulcers when not treated properly can lead to amputation and are ultimately life-threatening,” confirmed by Dr. Mrs. R.D. Rajeshwari from Sivasakthi Nursing Home in Chennai, Tamil Nadu, India. It is estimated that 15% of diabetic patients will develop foot ulcers and 6% will require hospitalization. DFUs are the most common cause of major non-traumatic amputation worldwide and the most costly type of chronic wound, with 84% of all diabetic-related amputations preceded by a Diabetic Foot Ulcer.

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DFU’s do not typically follow the expected acute wound healing phase progression, often becoming chronic wounds, especially when using traditional standard wound care of wet-dry treatments. Hyperglycemia and related factors such as advanced glycation end-products (AGEs) exacerbate peripheral neuropathy and angiopathy, which complicates healing. Several studies report that AGEs alter the interaction between cells and the extracellular matrix (ECM) and cause structural changes in collagen I.  AGE’s cause a stiffening of the tissues, limiting blood flow.

DFUs are also characterized by reduced growth factor production and decreased or impaired angiogenic response, macrophage function, collagen accumulation, and epidermal barrier function. The keratinocyte migration is inhibited because of the reduction and abnormal localization of endothelial growth factor receptors and the migration and proliferation of fibroblasts.

Collagen is the most abundant protein in the body, critical for structural support of the skin and ECM. Collagen’s unique triple-helical structure strengthens its scaffold function with Type I accounting for 80–85% of the collagen in the skin (5). Chronic wounds are characterized by elevated protease activity of metalloproteinases (MMPs) and serine proteases (e.g., human neutrophil elastase) that interfere with collagen synthesis, as well as growth factor release and action.

Dr Rohan Jain, President of Human BioSciences states, “Biotech innovations such as collagen have allowed us to directly interact with the wound by providing it with all the necessary materials it needs to heal itself. With this technology, patients will spend less time in the hospitals, endure fewer amputations, and pay less money for their healthcare.”

Collagen dressings can act as skin substitutes for the native extracellular matrix (ECM) to guide the complex cellular interaction necessary to prompt keratinocyte and fibroblast migration. The collagen is readily harvested from marine, bovine, porcine, ovine, and equine sources and mimics the native collagen in ECM. Collagen stabilizes the vascular and cellular components in the wound by reducing matrix metalloproteinases (MMP) levels that are typically imbalanced in chronic wounds while providing structural support for tissue repair  and regeneration.

Human BioSciences’ proprietary Kollagen™ technology protects and retains significantly more native triple helical protein structure, thus allowing superior stability of the molecule and scaffolding through all four phases of wound healing. All of Human Biosciences’ products contain native non-hydrolyzed Type -1 bovine collagen in its purest form. Currently, HBS offers three modes of delivery for KollagenTM technology:   Collatek® Gel, SkinTemp® II Sheets, and Medifil® II Collagen Particles

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