The transport of fluid and solute molecules in the interstitium is governed by the biological and physicochemical properties of the interstitial compartment as well as the physicochemical properties of the test molecule. The composition of the interstitial compartment of neoplastic tissues is significantly different from that of most normal tissues. In general the tumor interstitial compartment is characterized by large interstitial space, high collagen concentration, low proteoglycan and hyaluronate concentrations, high interstitial fluid pressure and flow, absence of anatomically well-defined functioning lymphatic network, high effective interstitial diffusion coefficient of macromolecules, as well as large hydraulic conductivity and interstitial convection compared to most normal tissues. While these factors favor movement of macromolecules in the tumor interstitium, high interstitial pressure and low microvascular pressure may retard extravasation of molecules and cells, especially in large tumors. These differences in transport parameters have major implications in tumor growth and metastases, as well as in tumor detection and treatment.

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Transport of Molecules in the Tumor Interstitium: A Review

Enzymatic Methods for the Determination of Small Quantities of Isomeric Chondroitin Sulfates

Accumulation and turnover of extracellular matrix components are the hallmarks of tissue injury. Fragmented hyaluronan stimulates the expression of inflammatory genes by a variety of immune cells at the injury site. Hyaluronan binds to a number of cell surface proteins on various cell types. Hyaluronan fragments signal through both Toll-like receptor (TLR) 4 and TLR2 as well as CD44 to stimulate inflammatory genes in inflammatory cells. Hyaluronan is also present on the cell surface of epithelial cells and provides protection against tissue damage from the environment by interacting with TLR2 and TLR4. Hyaluronan and hyaluronan-binding proteins regulate inflammation, tissue injury, and repair through regulating inflammatory cell recruitment, release of inflammatory cytokines, and cell migration. This review focuses on the role of hyaluronan as an immune regulator in human diseases.

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Hyaluronan as an Immune Regulator in Human Diseases

The Biochemistry of glycoproteins and proteoglycans

A hallmark of tissue injury and repair is the turnover of extracellular matrix components. This review focuses on the role of the glycosaminoglycan hyaluronan in tissue injury and repair. Both the synthesis and degradation of extracellular matrix are critical contributors to tissue repair and remodeling. Fragmented hyaluronan accumulates during tissue injury and functions in ways distinct from the native polymer. There is accumulating evidence that hyaluronan degradation products can stimulate the expression of inflammatory genes by a variety of immune cells at the injury site. CD44 is the major cell-surface hyaluronan receptor and is required to clear hyaluronan degradation products produced during lung injury; impaired clearance of hyaluronan results in persistent inflammation. However, hyaluronan fragment stimulation of inflammatory gene expression is not dependent on CD44 in inflammatory macrophages. Instead, hyaluronan fragments utilize both Toll-like receptor (TLR) 4 and TLR2 to stimulate inflammatory genes in macrophages. Hyaluronan also is present on the cell surface of lung alveolar epithelial cells and provides protection against tissue damage by interacting with TLR2 and TLR4 on these parenchymal cells. The simple repeating structure of hyaluronan appears to be involved in a number of important aspects of noninfectious tissue injury and repair that are dependent on the size and location of the polymer as well as the interacting cells. Thus, the interactions between the endogenous matrix component hyaluronan and its signaling receptors initiate inflammatory responses, maintain structural cell integrity, and promote recovery from tissue injury.

/pdf/hyaluronan-in-tissue-injury-and-repair-5fnd16at3e.pdf

Bernard Weissmann

Papers

The Structure of Hyalobiuronic Acid and of Hyaluronic Acid from Umbilical Cord1,2

The purine bases of human urine i. separation and identification

The transglycosylative action of testicular hyaluronidase.

The purine bases of human urine. II. Semiquantitative estimation and isotope incorporation.

Structure of hyaluronic acid. the glucuronidic linkage