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The Haversian canal contains the bone's blood supplies. The boundary of an osteon is the cement line. Each Haversian canal is surrounded by varying number (5-20) of concentrically arranged lamellae of bone matrix. Near the surface of the compact bone, the lamellae are arranged parallel to the surface; these are called circumferential lamellae.
The channels are formed by concentric layers called lamellae, which are approximately 50 μm in diameter. The Haversian canals surround blood vessels and nerve cells throughout bones and communicate with osteocytes (contained in spaces within the dense bone matrix called lacunae) through connections called canaliculi.
The lacuna are situated between the lamellae, and consist of a number of oblong spaces. In an ordinary microscopic section, viewed by transmitted light, they appear as fusiform opaque spots. Each lacuna is occupied during life by a branched cell, termed an osteocyte, bone-cell or bone-corpuscle.
Cancellous bone or spongy bone, [12] [11] also known as trabecular bone, is the internal tissue of the skeletal bone and is an open cell porous network that follows the material properties of biofoams. [13] [14] Cancellous bone has a higher surface-area-to-volume ratio than cortical bone and it is less dense. This makes it weaker and more flexible.
Bone broth is a great natural source of protein, says Millstine. Just one cup can pack 10 grams or more depending on the brand. The average person weighing 150 pounds needs 54 grams of protein a day .
Diameter of canaliculi in human bone is approximately 200 to 900 nm. [1] In bovine tibia diameter of canaliculi was found to vary from 155 to 844 nm (average 426 nm). [ 2 ] In mice humeri it varies from 80 to 710 nm (average 259 nm), while diameter of osteocytic processes varies from 50 to 410 nm (average 104 nm).
The cell also exhibits a reduced size endoplasmic reticulum, Golgi apparatus and mitochondria, and cell processes that radiate largely towards the bone surfaces in circumferential lamellae, or towards a haversian canal and outer cement line typical of osteons in concentric lamellar bone. [5]
Osteonectin is a 40 kDa acidic and cysteine-rich glycoprotein consisting of a single polypeptide chain that can be broken into 4 domains: 1) a Ca 2+ binding domain near the glutamic acid-rich region at the amino terminus (domain I), 2) a cysteine-rich domain (II), 3) a hydrophilic region (domain III), and 4) an EF hand motif at the carboxy terminus region (domain IV).