Arenicola marina extracellular hemoglobin (M101)

HEMOXYCarrier (M101) is a high-molecular-weight, extracellular hemoglobin derived from the marine lugworm Arenicola marina. Unlike mammalian hemoglobin, which is sequestered within red blood cells, M101 is naturally extracellular and possesses a massive hexagonal bilayer structure (approximately 3.6 MDa) comprising 156 globin chains and 144 oxygen-binding heme sites (Leize et al., 1996; Zal et al., 1997). Its primary biological function is the transport and delivery of molecular oxygen to tissues, operating independently of any specific cellular transporter or red blood cell environment (Rousselot et al., 2006). In therapeutic contexts, it is utilized as a Hemoglobin-Based Oxygen Carrier (HBOC) to treat conditions characterized by hypoxia or ischemia, such as during organ transplantation preservation or in the treatment of chronic wounds (Thuillier et al., 2011). The molecule's large size prevents it from passing through the vascular endothelium, thereby avoiding the vasoconstrictive side effects typically associated with smaller HBOCs that scavenge nitric oxide in the interstitial space. Additionally, M101 exhibits intrinsic superoxide dismutase-like activity, which helps mitigate oxidative stress during reperfusion injury (Hemarina, 2023).

Other names

HEMOXYCarrierLugworm hemoglobinM101HBL-HbHexagonal bilayer hemoglobinHEMO2life

Reversible binding of molecular oxygen to heme iron sites within the extracellular hemoglobin structure for delivery to hypoxic tissues via a passive diffusion gradient.